Amylin structure–function relationships and receptor pharmacology: implications for amylin mimetic drug development

Bower, Rebekah L; Hay, Debbie L

doi:10.1111/bph.13496

Cited by 104Neuropeptides and Animal PhysiologyDiabetes Treatment and ManagementPancreatic function and diabetes

Amylin structure–function relationships and receptor pharmacology: implications for amylin mimetic drug development

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Bower, Rebekah L, Hay, Debbie L·2016·British Journal of Pharmacology

DOI 10.1111/bph.13496PMC PMC4882495

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Abstract

Amylin is an important, but poorly understood, 37 amino acid glucoregulatory hormone with great potential to target metabolic diseases. A working example that the amylin system is one worth developing is the FDA‐approved drug used in insulin‐requiring diabetic patients, pramlintide. However, certain characteristics of pramlintide pharmacokinetics and formulation leave considerable room for further development of amylin‐mimetic compounds. Given that amylin‐mimetic drug design and development is an active area of research, surprisingly little is known about the structure/function relationships of amylin. This is largely due to the unfavourable aggregative and solubility properties of the native peptide sequence, which are further complicated by the composition of amylin receptors. These are complexes of the calcitonin receptor with receptor activity‐modifying proteins. This review explores what is known of the structure–function relationships of amylin and provides insights that can be drawn from the closely related peptide, CGRP. We also describe how this information is aiding the development of more potent and stable amylin mimetics, including peptide hybrids.

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Each receptor combination typically binds one calcitonin-family peptide with high affinity, while other family members bind same receptor dimer with lower affinities.
“Pharmacological studies of the interactions between peptides of the calcitonin family and their receptors have shown that each of the receptor combinations typically binds one of the calcitonin-family peptides with high affinity, whereas other members of the family can bind to the same receptor dimer with lower affinities (21).”
From The Activity of Peptides of the Calcitonin Family in Bone (2019) · cites this paper as [21]
The Amylin receptors and Amylin receptor pharmacology sections describe calcitonin-family peptides binding GPCR–RAMP receptor combinations and identify amylin as a high-affinity ligand at AMY1 and AMY3 receptors. They do not establish a general rule that each combination favors one peptide while all other family members bind with lower affinity: the pharmacology section reports that CGRP is also a potent agonist at some AMY receptors, with responses varying by RAMP and species (page not available in our copy). (LLM, conf=0.86)
Experimental — accuracy not yet measured
NH2-terminal and COOH-terminal are highly conserved among calcitonin, CGRP, and amylin, while middle region is more divergent.
“The NH 2 -terminal and COOH-terminal are highly conserved among calcitonin, CGPR, and amylin, whereas the middle region is more divergent (21).”
From The Activity of Peptides of the Calcitonin Family in Bone (2019) · cites this paper as [21]
Experimental — accuracy not yet measured
Linear peptides truncated at NH2-terminal, including amylin 8-37, alphaCGRP 8-37, and adrenomedullin 22-52, act as antagonists because they bind receptors but do not activate them.
“Thus, linear peptides produced by truncation of the NH 2terminal domains, including amylin 8 -37 , ␣CGRP 8 -37 , and adrenomedullin 22-52 , have been used as antagonists of the parent molecules, as they bind the receptors but fail to activate them (21).”
From The Activity of Peptides of the Calcitonin Family in Bone (2019) · cites this paper as [21]
IAPP is believed to interact with the calcitonin receptor (CALCR) but expression of CALCR is negligible in both mouse and human β-cells.
“IAPP is believed to interact with the calcitonin receptor (Calcr/CALCR) (84) but the expression of Calcr/CALCR expression is negligible in both mouse and human β-cells (Appendix Figure 12A).”
From Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men (2018) · cites this paper as [84]

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Hay, D. L., Harris, P. W. R., Kowalczyk, R., Brimble, M. A., Rathbone, D. L., Barwell, J., Conner, A. C., & Poyner, D. R. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12464 · Cited by 35 · see citing works
Self-citation
Selective CGRP and adrenomedullin peptide binding by tethered RAMP‐calcitonin receptor‐like receptor extracellular domain fusion proteins
Moad, H. E., & Pioszak, A. A. (2013) · Protein Science · doi:10.1002/pro.2377 · Cited by 34 · see citing works
Effect of Pramlintide on Postprandial Glucose Fluxes in Type 1 Diabetes
Hinshaw, L., Schiavon, M., Dadlani, V., Mallad, A., Man, C. D., Bharucha, A. E., Basu, R., Geske, J. R., Carter, R. E., Cobelli, C., et al. (2016) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2015-3952 · Cited by 32 · see citing works
Amylin and the Gastrointestinal Tract
Macdonald, I. A. (1997) · Diabetic Medicine · doi:10.1002/(sici)1096-9136(199706)14:2+ · Cited by 30 · see citing works
The role of the 8‐18 helix of CGRP8‐37 in mediating high affinity binding to CGRP receptors; coulombic and steric interactions
Howitt, S. G., Kilk, K., Wang, Y., Smith, D. M., Langel, Ü., & Poyner, D. R. (2003) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705040 · Cited by 29 · see citing works
Renal Elimination of Islet Amyloid Polypeptide
Leckström, A., Björklund, K., Permert, J., Larsson, R., & Westermark, P. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7465 · Cited by 29 · see citing works
Preparation and Characterization of PEGylated Amylin
Guerreiro, L. H., Guterres, M. F. A. N., Melo-Ferreira, B., Erthal, L. C. S., Rosa, M. D. S., Lourenço, D. C., Tinoco, P., & Lima, L. M. T. R. (2013) · AAPS PharmSciTech · doi:10.1208/s12249-013-9987-4 · Cited by 28 · see citing works
Synthesis and evaluation of disulfide bond mimetics of amylin-(1–8) as agents to treat osteoporosis
Kowalczyk, R., Harris, P. W. R., Brimble, M. A., Callon, K. E., Watson, M., & Cornish, J. (2012) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2012.02.030 · Cited by 27 · see citing works
Modifications to the N-Terminus but Not the C-Terminus of Calcitonin Gene-Related Peptide(8-37) Produce Antagonists with Increased Affinity
Smith, D. D., Saha, S. L., Fang, G., Schaffert, C. S., Waugh, D. J. J., Zeng, W., Tóth, G., Hulce, M., & Abel, P. W. (2003) · Journal of Medicinal Chemistry · doi:10.1021/jm020507f · Cited by 22 · see citing works
Bifunctional PEGylated Exenatide-Amylinomimetic Hybrids to Treat Metabolic Disorders: An Example of Long-Acting Dual Hormonal Therapeutics
Sun, C., Trevaskis, J. L., Jodka, C. M., Neravetla, S., Griffin, P. S., Xu, K., Wang, Y., Parkes, D. G., Forood, B., & Ghosh, S. S. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm401418s · Cited by 22 · see citing works
Molecular forms of islet amyloid polypeptide (IAPP/amylin) in four mammals
Miyazato, M., Nakazato, M., Shiomi, K., Aburaya, J., Kangawa, K., Matsuo, H., & Matsukura, S. (1992) · Diabetes Research and Clinical Practice · doi:10.1016/0168-8227(92)90064-x · Cited by 20 · see citing works
The effects of C-terminal truncation of receptor activity modifying proteins on the induction of amylin receptor phenotype from human CTb receptors
Udawela, M., Christopoulos, G., Morfis, M. M., Tilakaratne, N., Christopoulos, A., & Sexton, P. M. (2007) · Regulatory Peptides · doi:10.1016/j.regpep.2007.08.003 · Cited by 15 · see citing works
Amylin-Based Pharmacotherapy – Past, Present & Future
Roth, J. D., Mack, C. M., Soares, C., Ghosh, S. S., & Parkes, D. G. (2008) · Immunology Endocrine & Metabolic Agents - Medicinal Chemistry · doi:10.2174/187152208787169189 · Cited by 15 · see citing works
Molecular model-building of amylin and α-calcitonin gene-related polypeptide hormones using a combination of knowledge sources
Saldanha, J. W., & Mahadevan, D. (1991) · Protein Engineering Design and Selection · doi:10.1093/protein/4.5.539 · Cited by 15 · see citing works
Structural comparison of alanine‐substituted analogues of the calcitonin gene‐related peptide 8‐37 Importance of theC‐terminal segment for antagonistic activity
Boulanger, Y., Khiat, A., LAROCQUE, A., Fournier, A., & St-Pierre, S. A. (1996) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1996.tb01098.x · Cited by 14 · see citing works
Nephrectomy Decreases Amylin and Pramlintide Clearance in Rats
Vine, W., Smith, P., LaChappell, R., Blase, E., Lumpkin, R., & Young, A. (1998) · Hormone and Metabolic Research · doi:10.1055/s-2007-978923 · Cited by 14 · see citing works
Increased levels of plasma amylin in advanced renal failure.
Watschinger, B., Hartter, E., Traindl, O., Pohanka, E., Pidlich, J., & Kovařík, J. (1992) · PubMed · Cited by 10 · see citing works
Amylin Conjugation with Methoxyl Polyethyleneglycol
Guterres, M. F. A. N., Guerreiro, L. H., Melo-Ferreira, B., Erthal, L. C. S., & Lima, L. T. R. (2013) · Protein and Peptide Letters · doi:10.2174/09298665113209990067 · Cited by 9 · see citing works
The calcitonin gene-related peptide family
Hay, D. L., & Dickerson, I. M. (2009) · Springer eBooks · doi:10.1007/978-90-481-2909-6 · Cited by 9 · see citing works
Self-citation
Aspects of structural landscape of human islet amyloid polypeptide
He, J., Dai, J., Li, J., Peng, X., & Niemi, A. J. (2015) · The Journal of Chemical Physics · doi:10.1063/1.4905586 · Cited by 8 · see citing works
Isolation and sequence determination of two N-terminal fragments of islet amyloid polypeptide in rat pancreas
Miyazato, M., Nakazato, M., Shiomi, K., Kangawa, K., Matsuo, H., & Matsukura, S. (1994) · Regulatory Peptides · doi:10.1016/0167-0115(94)90142-2 · Cited by 7 · see citing works
Synthesis and Structure‐Activity Analysis of Fragments and Analogs of CGRP8‐37a
Mimeault, M., St-Pierre, S. A., Quirion, R., Dumont, Y., & Fournier, A. (1992) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1992.tb22790.x · Cited by 5 · see citing works
Biotinyl analogues of amylin as biologically active probes for amylin/CGRP receptor recognition
Chantry, A., FOOT, E. A., Leighton, B., Day, A. J., & Willis, A. C. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80362-k · Cited by 3 · see citing works
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Barbero (2014) · doi:10.1016/j · Cited by 1 · see citing works

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Anti-obesity drug discovery: advances and challenges
Müller, T. D., Blüher, M., Tschöp, M. H., & DiMarchi, R. D. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00337-8 · Cited by 1,021 · see citing works
Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men
Rorsman, P., & Ashcroft, F. M. (2018) · Physiological Reviews · doi:10.1152/physrev.00008.2017 · Cited by 793 · see citing works
Update on the pharmacology of calcitonin/CGRP family of peptides: IUPHAR Review 25
Hay, D. L., Garelja, M. L., Poyner, D. R., & Walker, C. S. (2017) · British Journal of Pharmacology · doi:10.1111/bph.14075 · Cited by 375 · see citing works
“…two peptides, the first residues N-terminal to the disulphide bond do not appear to be necessary for biological activity, and the AM and AM2/IMD peptides can be considered as functional ~40 amino acid peptides (Bailey and Hay, 2006; Hong et al., 2012; Watkins et al., 2013; Bower and Hay, 2016).”
BackgroundInfluentialSelf-citation
The Activity of Peptides of the Calcitonin Family in Bone
Naot, D., Musson, D. S., & Cornish, J. (2019) · Physiological Reviews · doi:10.1152/physrev.00066.2017 · Cited by 141 · see citing works
“The NH2-terminal and COOH-terminal are highly conserved among calcitonin, CGPR, and amylin, whereas the middle region is more divergent (21).”
Background
Amylin - its role in the homeostatic and hedonic control of eating and recent developments of amylin analogs to treat obesity
Boyle, C. N., Lutz, T. A., & Le Foll, C. (2018) · Molecular Metabolism · doi:10.1016/j.molmet.2017.11.009 · Cited by 142 · see citing works
“On the other hand, transfected cell system studies show that amylin signaling also involves cAMP, intracellular Ca2þ, and beta-arrestin [17,22].”
Background
Calcitonin Gene‐Related Peptide Modulators – The History and Renaissance of a New Migraine Drug Class
Hargreaves, R. J., & Olesen, J. (2019) · Headache The Journal of Head and Face Pain · doi:10.1111/head.13510 · Cited by 129 · see citing works
Expression of the CGRP Family of Neuropeptides and their Receptors in the Trigeminal Ganglion
Edvinsson, L. I., Grell, A.-S., & Warfvinge, K. (2020) · Journal of Molecular Neuroscience · doi:10.1007/s12031-020-01493-z · Cited by 93 · see citing works
Molecular Signature for Receptor Engagement in the Metabolic Peptide Hormone Amylin
Bower, R. L., Yule, L. R., Rees, T. A., Deganutti, G., Hendrikse, E. R., Harris, P. W. R., Kowalczyk, R., Ridgway, Z. M., Wong, A. G., Swierkula, K., et al. (2018) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.8b00002 · Cited by 80 · see citing works
Self-citation
Calcitonin and Bone Physiology: In Vitro, In Vivo, and Clinical Investigations
Xie, J., Guo, J., Kanwal, Z., Wu, M., Lv, X., Ibrahim, N. A., Li, P., Buabeid, M. A., Arafa, E. A., & Sun, Q. (2020) · International Journal of Endocrinology · doi:10.1155/2020/3236828 · Cited by 73 · see citing works
“Among all calcitonin, CGPR, and amylin, the NH2 and COOH terminal remain preserved, while the middle area grows in a different direction [49].”
Background
Islet Amyloid Polypeptide: A Partner in Crime With Aβ in the Pathology of Alzheimer's Disease
Raimundo, A., Ferreira, S., Martins, I. C., & Menezes, R. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00035 · Cited by 71 · see citing works
“To yield the mature active form of the hormone, IAPP suffers amidation of the Cterminal end, and a disulphide bond is formed between cysteines at positions two and seven (Westermark et al., 2011; Akter et al., 2016; Bower and Hay, 2016).”
Background
Amylin brain circuitry
Boccia, L., Gamakharia, S., Coester, B., Whiting, L., Lutz, T. A., & Le Foll, C. (2020) · Peptides · doi:10.1016/j.peptides.2020.170366 · Cited by 70 · see citing works
“The amylin peptide sequence is very well conserved across species [6] and the difference in amino acid sequence between humans and cats versus rodents prevents rodents amylin to aggregate [7].”
Creating the amylin story
Lutz, T. A. (2022) · Appetite · doi:10.1016/j.appet.2022.105965 · Cited by 59 · see citing works
Amylin and Leptin: Co-Regulators of Energy Homeostasis and Neuronal Development
Levin, B. E., & Lutz, T. A. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2016.11.004 · Cited by 49 · see citing works
Amylin
Hay, D. L. (2017) · Headache The Journal of Head and Face Pain · doi:10.1111/head.13077 · Cited by 42 · see citing works
“Nevertheless, the conserved threonine at position 6 in all calcitonin family peptides is essential for receptor activation in CGRP at the CGRP and AMY1 receptors.(3,22) This supports the hypothesis that both are endogenous CGRP receptors.”
Self-citation
Metal-dependent hormone function: the emerging interdisciplinary field of metalloendocrinology
Stevenson, M. J., Uyeda, K. S., Harder, N. H. O., & Heffern, M. C. (2018) · Metallomics · doi:10.1039/c8mt00221e · Cited by 41 · see citing works
Amylin, Another Important Neuroendocrine Hormone for the Treatment of Diabesity
Eržen, S., Tonin, G., Jurišić‐Eržen, D., & Klen, J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031517 · Cited by 38 · see citing works
“In blood, it can be found in non-glycosylated and glycosylated forms, with the latter inactive in blood [12,13].”
Background
Prediction Methods of Herbal Compounds in Chinese Medicinal Herbs
Han, K., Zhang, L., Wang, M., Zhang, R., Wang, C., & Zhang, C. (2018) · Molecules · doi:10.3390/molecules23092303 · Cited by 38 · see citing works
A nexus of miR-1271, PAX4 and ALK/RYK influences the cytoskeletal architectures in Alzheimer's Disease and Type 2 Diabetes
Majumder, P., Chanda, K., Das, D., Singh, B. K., Chakrabarti, P., Jana, N. R., & Mukhopadhyay, D. (2021) · Biochemical Journal · doi:10.1042/bcj20210175 · Cited by 38 · see citing works
“Amylin is a Calcitonin family peptide and it tends to interact with GPCRs of class B [25] in non-disease conditions.”
Human islet amyloid polypeptide: A therapeutic target for the management of type 2 diabetes mellitus
Roham, P. H., Save, S. N., & Sharma, S. (2022) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2022.04.001 · Cited by 37 · see citing works
CGRP, Amylin, Immunology, and Headache Medicine
Taylor, F. R. (2018) · Headache The Journal of Head and Face Pain · doi:10.1111/head.13432 · Cited by 30 · see citing works
Automated detection of squint as a sensitive assay of sex-dependent calcitonin gene–related peptide and amylin-induced pain in mice
Rea, B. J., Davison, A., Ketcha, M.-J., Smith, K. J., Fairbanks, A. M., Wattiez, A., Poolman, P., Kardon, R. H., Russo, A. F., & Sowers, L. P. (2021) · Pain · doi:10.1097/j.pain.0000000000002537 · Cited by 30 · see citing works
Amylin in Alzheimer's disease: Pathological peptide or potential treatment?
Mietlicki‐Baase, E. G. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.12.016 · Cited by 29 · see citing works
“RAMP1) and AMY3A (CTR-A/RAMP3) are most well characterized (Bailey et al., 2012; Bower and Hay, 2016).”
Background
Amylin Receptor: A Potential Therapeutic Target for Alzheimer’s Disease
Fu, W., Patel, A., Kimura, R., Soudy, R., & Jhamandas, J. H. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.06.003 · Cited by 28 · see citing works
Subclinical Diabetes
Lima, L. M. T. R. (2017) · Anais da Academia Brasileira de Ciências · doi:10.1590/0001-3765201720160394 · Cited by 27 · see citing works
Neuroprotective Effects of the Amylin Analog, Pramlintide, on Alzheimer’s Disease Are Associated with Oxidative Stress Regulation Mechanisms
Patrick, S., Corrigan, R. R., Grizzanti, J., Mey, M., Blair, J., Pallàs, M., Camins, A., Lee, H., & Casadesús, G. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-180421 · Cited by 27 · see citing works
“…correlation between plasma and cerebrospinal ﬂuid amylin levels and cognitive function in T2DM [28], AD, and MCI patients [29, 30]; pre-clinical studies also demonstrated the neuroprotective beneﬁts of amylin and pramlintide (PRAM), a non-aggregating synthetic analogue derived from rat amylin [31].”
A selective role for receptor activity‐modifying proteins in subchronic action of the amylin selective receptor agonist NN1213 compared with salmon calcitonin on body weight and food intake in male mice
Arrigoni, S., Foll, C. L., Cabak, A., Lundh, S. H., Raun, K., John, L. M., & Lutz, T. A. (2021) · European Journal of Neuroscience · doi:10.1111/ejn.15376 · Cited by 27 · see citing works
“Amylin is a centrally acting peptide hormone coproduced and cosecreted with insulin by pancreatic β cells in response to nutrient influx in the gastrointestinal tract (Bower & Hay, 2016; Cooper, 1994).”
Background
Amylin: From Mode of Action to Future Clinical Potential in Diabetes and Obesity
Volčanšek, Š., Koceva, A., Jensterle, M., Janež, A., & Muzurović, E. M. (2025) · Diabetes Therapy · doi:10.1007/s13300-025-01733-8 · Cited by 26 · see citing works
“Furthermore, the ability of amylin receptors to interact with other peptides, such as CT and CGRP, adds another layer of complexity to their signaling and functional roles [29, 30, 33].”
Influential
Amylin Modulates a Ventral Tegmental Area–to–Medial Prefrontal Cortex Circuit to Suppress Food Intake and Impulsive Food-Directed Behavior
Geisler, C. E., Décarie-Spain, L., Loh, M. K., Trumbauer, W., Gaisinsky, J., Klug, M. E., Pelletier, C., Davis, J. F., Schmidt, H. D., Roitman, M. F., et al. (2023) · Biological Psychiatry · doi:10.1016/j.biopsych.2023.07.011 · Cited by 24 · see citing works
Amyloidogenicity, Cytotoxicity, and Receptor Activity of Bovine Amylin: Implications for Xenobiotic Transplantation and the Design of Nontoxic Amylin Variants
Akter, R., Bower, R. L., Abedini, A., Schmidt, A. M., Hay, D. L., & Raleigh, D. P. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00690 · Cited by 23 · see citing works
Self-citation
Distributed amylin receptor signaling and its influence on motivated behavior
Kern, K. A., & Mietlicki‐Baase, E. G. (2020) · Physiology & Behavior · doi:10.1016/j.physbeh.2020.112958 · Cited by 20 · see citing works
Structural insight into selectivity of amylin and calcitonin receptor agonists
Cao, J., Belousoff, M. J., Gerrard, E. J., Danev, R., Fletcher, M. M., Maso, E. D., Schreuder, H., Lorenz, K., Evers, A., Tiwari, G., et al. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01393-4 · Cited by 20 · see citing works
“The single lysine substitution at position 20, 21 or 22 had little effect on the potency of analogs for either receptor.”
Influential
Whole‐brain mapping of amylin‐induced neuronal activity in receptor activity–modifying protein 1/3 knockout mice
Skovbjerg, G., Roostalu, U., Hansen, H. H., Lutz, T. A., Foll, C. L., Salinas, C. G., Skytte, J. L., Jelsing, J., Vrang, N., & Hecksher‐Sørensen, J. (2021) · European Journal of Neuroscience · doi:10.1111/ejn.15254 · Cited by 19 · see citing works
“Development of amylin analogues for treatment of metabolic diseases is complicated by the complex receptor biology of amylin (Bower & Hay, 2016).”
Background
Physico-chemical properties of co-formulated fast-acting insulin with pramlintide
da Silva, D. C., & Lima, L. M. T. R. (2018) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2018.06.039 · Cited by 19 · see citing works
“Others amylin analogues, hybrids and receptors agonists are currently found in pipeline of development (Bower and Hay, 2016; Riddle and Drucker, 2006), demonstrating the interest and importance of amylin physiology and pharmacology.”
Background
Novel Pharmaceuticals in Appetite Regulation: Exploring emerging gut peptides and their pharmacological prospects
Rubinić, I., Kurtov, M., & Likić, R. (2024) · Pharmacology Research & Perspectives · doi:10.1002/prp2.1243 · Cited by 22 · see citing works
“192-194 The main limitation of human amylin is its short half-life, a result of renal clearance and proteolysis, 195 as well as its propensity to aggregate into fibrils that have no therapeutic value and are even harmful.”
Background
BZ043, a novel long-acting amylin analog, reduces gastric emptying, food intake, glycemia and insulin requirement in streptozotocin-induced diabetic rats
do Nascimento, C. V. M. F., Sinézia, C., Sisnande, T., Lima, L. M. T. R., & Lacativa, P. G. S. (2019) · Peptides · doi:10.1016/j.peptides.2019.04.004 · Cited by 18 · see citing works
Fremanezumab for the preventive treatment of migraine in adults
Lionetto, L., Curto, M., Cisale, G. Y., Capi, M., Cipolla, F., Guglielmetti, M., & Martelletti, P. (2019) · Expert Review of Clinical Pharmacology · doi:10.1080/17512433.2019.1635452 · Cited by 18 · see citing works
“Amylin (AMY) or islet amyloid polypeptide (IAPP) is a neuroendocrine hormone produced by beta cells of pancreatic islets in co-secretion with insulin [28].”
Background
Activation of the amylin pathway modulates cocaine-induced activation of the mesolimbic dopamine system in male mice
Kalafateli, A. L., Aranäs, C., & Jerlhag, E. (2020) · Hormones and Behavior · doi:10.1016/j.yhbeh.2020.104885 · Cited by 18 · see citing works
Safety, tolerability and pharmacokinetic characterisation of DACRA KBP‐042 in healthy male subjects
Henriksen, K., Broekhuizen, K., de Boon, W. M. I., Karsdal, M. A., Bihlet, A. R., Christiansen, C., Dillingh, M. R., de Kam, M., Kumar, R., Burggraaf, J., et al. (2021) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.14921 · Cited by 17 · see citing works
“Twelve (12) subjects were excluded based on the inclusion and exclusion criteria.”
Salmon Calcitonin Attenuates Some Behavioural Responses to Nicotine in Male Mice
Aranäs, C., Vestlund, J., Witley, S., Edvardsson, C. E., Kalafateli, A. L., & Jerlhag, E. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.685631 · Cited by 17 · see citing works
The Calcitonin/Calcitonin Gene-Related Peptide Family in Invertebrate Deuterostomes
Sekiguchi, T. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00695 · Cited by 17 · see citing works
“Comparisons of each CT/CGRP family peptide members in the same vertebrate spices show low primary amino acid sequence identity, whereas these peptides share common secondary amino acid structures such as the N-terminal circular structure formed by a disulfide bond, α-helical structure following the N-terminal region,…”
Background
The Structural Refinement of Glucagon for Therapeutic Use.
Chabenne, J. R., Mroz, P., Mayer, J., & DiMarchi, R. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01493 · Cited by 14 · see citing works
Systemic and Central Amylin, Amylin Receptor Signaling, and Their Physiological and Pathophysiological Roles in Metabolism
Foll, C. L., & Lutz, T. A. (2020) · Comprehensive physiology · doi:10.1002/cphy.c190034 · Cited by 27 · see citing works
Pramlintide an Adjunct to Insulin Therapy: Challenges and Recent Progress in Delivery
Pradyuth, K. S., Kumar, A., Chitkara, D., & Mittal, A. (2023) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.123.001679 · Cited by 13 · see citing works
Converting the Amyloidogenic Islet Amyloid Polypeptide into a Potent Nonaggregating Peptide Ligand by Side Chain-to-Side Chain Macrocyclization
Babych, M., Garelja, M. L., Nguyen, P. T., Hay, D. L., & Bourgault, S. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c05297 · Cited by 13 · see citing works
Self-citation
The story of amylin: from physiology to therapy
Secher, A., Lutz, T. A., & Raun, K. (2026) · Nature Metabolism · doi:10.1038/s42255-026-01465-4 · Cited by 12 · see citing works
“As mentioned, native amylin has a strong propensity to aggregate into amyloid fibrils, complicating its formulation and stability 33,197 , and overcoming this fibrillation tendency has been central to designing clinically viable analogues 43,198 .”
Calcitonin receptor signaling in nucleus accumbens D1R- and D2R-expressing medium spiny neurons bidirectionally alters opioid taking in male rats
Zhang, Y., Nathan, J. B., Moreno, A., Merkel, R., Kahng, M. W., Hayes, M. R., Reiner, B. C., Crist, R. C., & Schmidt, H. D. (2023) · Neuropsychopharmacology · doi:10.1038/s41386-023-01634-z · Cited by 12 · see citing works
The calcitonin receptor is the main mediator of LAAMA's body weight lowering effects in male mice
Gamakharia, S., Foll, C. L., Rist, W., Baader-Pagler, T., Baljuls, A., & Lutz, T. A. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174352 · Cited by 11 · see citing works
“It is important to consider that even though the increase of intracellular cAMP after LAAMA or amylin treatment means that the receptor has been activated in vitro (Bower and Hay, 2016), it is not always accompanied by an anorectic effect in vivo (Hay et al.”
Background
The unique pathophysiological features of diabetes mellitus secondary to total pancreatectomy: proposal for a new classification distinct from diabetes of the exocrine pancreas
Infante, M., & Ricordi, C. (2023) · Expert Review of Endocrinology & Metabolism · doi:10.1080/17446651.2023.2168645 · Cited by 10 · see citing works
“islet amyloid polypeptide or IAPP) which is co-secreted with insulin by pancreatic beta cells in response to meals and at a molar ratio of approximately 1:100 (amylin-to-insulin) [71,72].”
Background
Human IAPP is a contributor to painful diabetic peripheral neuropathy
Albariqi, M. M. H., Versteeg, S., Brakkee, E. M., Coert, J., Elenbaas, B. O. W., Prado, J., Hack, C., Höppener, J., & Eijkelkamp, N. (2021) · bioRxiv · doi:10.1172/jci156993 · Cited by 8 · see citing works
“Since hIAPP has a very short half-life (few minutes) (13), these data indicate that a short but strong rise in systemic hIAPP concentration is sufficient to cause long-lasting changes in peripheral sensory neurons.”
Background
Systemic and Central Amylin, Amylin Receptor Signaling, and Their Physiological and Pathophysiological Roles in Metabolism
Foll, C. L., & Lutz, T. A. (2020) · Comprehensive physiology · doi:10.1002/j.2040-4603.2020.tb00140.x · Cited by 10 · see citing works
“Amylin receptor pharmacology is complex because several distinct amylin receptor subtypes have been described (10, 41, 104); the prototypical amylin receptors 1 to 3 are thought to be derived from the co-expression of the calcitonin core receptor (CTR) with receptor-activity modifying proteins…”
The processing intermediate of human amylin, pro-amylin(1–48), has in vivo and in vitro bioactivity
Mazzini, G., Foll, C. L., Boyle, C. N., Garelja, M. L., Zhyvoloup, A., Miller, M. E. T., Hay, D. L., Raleigh, D. P., & Lutz, T. A. (2024) · Biophysical Chemistry · doi:10.1016/j.bpc.2024.107201 · Cited by 9 · see citing works
Self-citation
Role of amylin in feeding and satiation
Lutz, T. A. (2025) · Neuropharmacology · doi:10.1016/j.neuropharm.2025.110587 · Cited by 9 · see citing works
“…receptor specificity and affinity; further, they may also be involved in controlling the transport of the receptor complexes to the cell surface(Bower and Hay, 2016; Christopoulos et al., 1999; Fischer et al., 2002; Fletcher et al., 2021; Hay et al., 2005, 2015, 2016; Keov et al., 2024; Le…”
In Silico Comparative Study of Human and Porcine Amylin
Alves, N. A., & Frigori, R. B. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b09363 · Cited by 9 · see citing works
Update on: effects of anti-diabetic drugs on bone metabolism
Mabilleau, G., & Bouvard, B. (2020) · Expert Review of Endocrinology & Metabolism · doi:10.1080/17446651.2020.1831911 · Cited by 9 · see citing works
On the importance of being amidated: Analysis of the role of the conserved C-terminal amide of amylin in amyloid formation and cytotoxicity
Yang, T., Filippov, I., Manathunga, L., Baghai, A., Maréchal, A., Raleigh, D. P., & Zhyvoloup, A. (2024) · Biophysical Chemistry · doi:10.1016/j.bpc.2023.107168 · Cited by 8 · see citing works
Role of mass spectrometry in the study of interactions between amylin and metal ions
Moracci, L., Crotti, S., Traldi, P., Agostini, M., Cosma, C., & Lapolla, A. (2021) · Mass Spectrometry Reviews · doi:10.1002/mas.21732 · Cited by 8 · see citing works
Islet amyloid polypeptide does not suppress pancreatic cancer
Taylor, A. J., Panzhinskiy, E., Orban, P. C., Lynn, F. C., Schaeffer, D. F., Johnson, J. D., Kopp, J. L., & Verchere, C. B. (2023) · Molecular Metabolism · doi:10.1016/j.molmet.2023.101667 · Cited by 7 · see citing works
“IAPP receptors are generated through heterodimerization of the calcitonin receptor (CALCR; CTR) with one of three receptor activitymodifying protein family members (RAMP-1,-2, or-3) which increase specificity of the receptors for IAPP [31].”
Background
Amylin and the amylin receptors in migraine: Is there another pathway to target?
Moreno‐Ajona, D., Gosalia, H., Hoffmann, J., & Goadsby, P. J. (2025) · Cephalalgia · doi:10.1177/03331024251340066 · Cited by 7 · see citing works
“It is a high-af ﬁ nity ligand for the AMY 1 and AMY 3 receptors, variable of AMY 2 (6,10) .”
Design, synthesis and preclinical evaluation of bio-conjugated amylinomimetic peptides as long-acting amylin receptor agonists
Patch, R. J., Zhang, R., Edavettal, S. C., Macielag, M. J., Eckardt, A. J., Li, J., Rives, M., Edwards, W., Hinke, S. A., Qiu, X., et al. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114330 · Cited by 7 · see citing works
Synergistic long-range effects of mutations underlie aggregation propensities of amylin analogues
Alves, N. A., Dias, L. G., & Frigori, R. B. (2019) · Journal of Molecular Modeling · doi:10.1007/s00894-019-4137-x · Cited by 7 · see citing works
Long-acting amylin-related peptides as therapies for obesity and type 2 diabetes
Bailey, C. J., Flatt, P. R., & Conlon, J. M. (2026) · Peptides · doi:10.1016/j.peptides.2026.171480 · Cited by 6 · see citing works
Type‐2 Diabetes, Pancreatic Amylin, and Neuronal Metabolic Remodeling in Alzheimer's Disease
Leibold, N. S., Bain, J. R., & Despa, F. (2023) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202200405 · Cited by 6 · see citing works
Amylin Pharmacology in Alzheimer’s Disease Pathogenesis and Treatment
Casadesus, G., Corrigan, R. R., & Piontkivska, H. (2021) · Current Neuropharmacology · doi:10.2174/1570159x19666211201093147 · Cited by 6 · see citing works
“Additional sites of amylin of binding as well as amylin uptake, confirmed amylin-labeled radioactivity include: ventral tegmental area (VTA), hypothalamus, NAc, subfornical organ (SFO), amygdala, bed nucleus of the stria terminalis (BNST), locus coeruleus, thalamus pons, medulla, hippocampus, striatum, as well as fron…”
Cryo-EM exposes diverse polymorphism in IAPP mutants to guide the rational design of peptide-based therapeutics
Ooi, S. A., Valli, D., Kuska, M. I., Marí, H., Chaudhary, H., Wahlgren, W. Y., Westenhoff, S., Tietze, A. A., Novials, A., Servitja, J., et al. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169405 · Cited by 5 · see citing works
“16 Consequently, the search for improved formulation is still on-going, with new promising IAPP analogs undergoing clinical trials.”
Neuroprotective Mechanisms of Amylin Receptor Activation, Not Antagonism, in the APP/PS1 Mouse Model of Alzheimer’s Disease
Corrigan, R. R., Labrador, L., Grizzanti, J., Mey, M., Piontkivska, H., & Casadesús, G. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-221057 · Cited by 5 · see citing works
Is the activity of CGRP and Adrenomedullin regulated by RAMP (−2) and (−3) in Trypanosomatidae? An in-silico approach
Febres-Aldana, A. J., Vanegas, O., Giammarresi, M., Gomes, C., Dı́az, E., & Ponte‐Sucre, A. (2018) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2018.04.003 · Cited by 5 · see citing works
Structural effects driven by rare point mutations in amylin hormone, the type II diabetes-associated peptide
Mendes, W. S., Franco, O. L., de Alencar, S. A., & Porto, W. F. (2021) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2021.129935 · Cited by 5 · see citing works
Molecular engineering of designer diabetes therapeutics
DeWolf, E. L., Webber, B., & Webber, M. J. (2026) · Journal of Controlled Release · doi:10.1016/j.jconrel.2026.114705 · Cited by 4 · see citing works
L’îlot pancréatique : ce que nous savons 150 ans après Langerhans
Mandarim-de-Lacerda, C. A. (2019) · Bulletin de l'Académie Nationale de Médecine · doi:10.1016/j.banm.2019.06.015 · Cited by 6 · see citing works
Engineering of an Ultralong-Acting and Nonaggregating Dual Amylin and Calcitonin Receptor Agonist with Durable Efficacy in Obesity and Diabetes
Zheng, N., Chen, R., Yang, L., Xu, P., Wang, X., Sun, X., Lin, Y.-X., Qiu, J., Su, X., Wang, Y., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c02893 · Cited by 3 · see citing works
Calcitonin peptides
Naot, D., Musson, D. S., & Cornish, J. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814841-9.00033-6 · Cited by 4 · see citing works
Impact of Gut and Metabolic Hormones on Feeding Reward
Klockars, A., Levine, A. S., Head, M. A., Perez‐Leighton, C. E., Kotz, C. M., & Olszewski, P. K. (2021) · Comprehensive physiology · doi:10.1002/cphy.c190042 · Cited by 5 · see citing works
Peripheral amylin modulation rebalances brain glycolysis and Tau-Ser214 phosphorylation via cAMP-PKA signaling
Davargaon, R. S., Verma, N., Kotiya, D., Leibold, N. S., Velmurugan, G. V., Ly, H., Chen, K. C., Ruíz, D., Corces, V. G., Liu, H., et al. (2026) · iScience · doi:10.1016/j.isci.2026.115157 · Cited by 2 · see citing works
The Bioenergetic Architecture of Metabolic Regulation: From Gut–Brain Signalling to Next-Generation Peptide Pharmacology
Rega, M., Petraglia, F. M., D’Ursi, L., Buonocore, M., Criscuolo, D., & Santoro, A. (2026) · Clinical bioenergetics · doi:10.3390/clinbioenerg2010005 · Cited by 2 · see citing works
“Amylin, also known as islet amyloid polypeptide (IAPP) or diabetes-associated peptide, is a member of the calcitonin (CT) family of peptides [100].”
Massively parallel quantification of mutational impact on IAPP amyloid formation
Badia, M., Batlle, C., & Bolognesi, B. (2026) · Nature Communications · doi:10.1038/s41467-026-70611-z · Cited by 2 · see citing works
“Different structural polymorphs have been described for ﬁ brils formed by the two peptides in vitro or extracted from human tissue (8 for IAPP 14,19 – 23 and 10 for A β 42 24 – 29 ).”
Impact of Gut and Metabolic Hormones on Feeding Reward
Klockars, A., Levine, A. S., Head, M. A., Perez‐Leighton, C. E., Kotz, C. M., & Olszewski, P. K. (2021) · Comprehensive physiology · doi:10.1002/j.2040-4603.2021.tb00153.x · Cited by 2 · see citing works
Female mice exhibit a more sensitive automated squint response to pain induced by CGRP and amylinPreprint
Rea, B. J., Sowers, L. P., Davison, A., Fairbanks, A. M., Wattiez, A., Poolman, P., Kardon, R. H., & Russo, A. F. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.26.445893 · Cited by 2 · see citing works
“Human amylin has ~50% sequence identity with CGRP and the two peptides bind a shared receptor (AMY1) with equal affinity [2].”
Background
The CGRP Family of Neuropeptides and their Receptors in the Trigeminovascular System
Edvinsson, L. I., & Warfvinge, K. (2021) · Headache · doi:10.1007/978-3-030-69032-8_1 · Cited by 1 · see citing works
Molecular and Cellular Mechanisms of CGRP Antagonists
Haanes, K. A., & Edvinsson, L. I. (2022) · Headache · doi:10.1007/978-3-030-95334-8_2 · Cited by 1 · see citing works
Changes in hippocampal volume, synaptic plasticity and amylin sensitivity in an animal model of type 2 diabetes are associated with increased vulnerability to amyloid-beta in advancing age
Tarhan, M., Hartl, T., Shchyglo, O., Colitti-Klausnitzer, J., Kuhla, A., Breuer, T. M., & Manahan‐Vaughan, D. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1373477 · Cited by 1 · see citing works
“Amylin is a 37-amino acid neuroendocrine polypeptide hormone that is co-secreted with insulin from pancreatic β - cells (Westermark et al., 2011; Bower and Hay, 2016).”
Background
Amylin Analogs: The Next Major Class of Weight Loss Therapy: A Review of Experimental Data and Early‐Phase Clinical Trials
Alhazmi, A., & le Roux, C. W. (2026) · Diabetes Obesity and Metabolism · doi:10.1111/dom.71074 · Cited by 1 · see citing works
Noncardiovascular-derived therapeutic peptidomimetics in cardiovascular disease
Litmanovich, A., Ertracht, O., Blumberg, Y., Saad, M., Moady, G., & Qvit, N. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-820141-1.00013-3 · Cited by 1 · see citing works
Peripheral Modulators of Appetite in Eating Disorders
Procházková, P., Roubalová, R., & Papežová, H. (2023) · Springer eBooks · doi:10.1007/978-3-030-97416-9_113-1 · Cited by 1 · see citing works
Structural Analysis of Amylin and Amyloid β Peptide Signaling in Alzheimer’s Disease
Xie, L., Lockhart, C., Bowers, S. R., Klimov, D. K., & Jafri, M. S. (2025) · Biomolecules · doi:10.3390/biom15010089 · Cited by 1 · see citing works
Structure, Self-Association, and Aggregation Properties of a Long-Acting Amylin Receptor Agonist
Poulsen, C., Norrman, M., Thomsen, J. K., & Wahlund, P. (2025) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.5c00161 · Cited by 1 · see citing works
Amylin and amylin receptors in Alzheimer's disease
Fu, W., & Jhamandas, J. H. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815868-5.00020-7 · Cited by 1 · see citing works
An electrospray ionization study on complexes of amylin with Cu(II) and Cu(I)
Moracci, L., Crotti, S., Traldi, P., Cosma, C., Lapolla, A., Pucciarelli, S., & Agostini, M. (2021) · Journal of Mass Spectrometry · doi:10.1002/jms.4773 · Cited by 1 · see citing works
Amylin regulates testosterone levels via steroidogenesis-related enzymes in the central nervous system of male mice
Chen, Y., Li, Q., Li, X., Liu, H., Li, P., Hai, R., Guo, Y., Wang, S., Wang, K., & Du, C. (2022) · Neuropeptides · doi:10.1016/j.npep.2022.102288 · Cited by 1 · see citing works
Physico-chemical properties of co-formulation of insulin with pramlintidePreprint
da Silva, D. C., & Lima, L. M. T. R. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/227363 · Cited by 1 · see citing works
“analogues, hybrids and receptors agonists are currently found in pipeline of development (24,25).”
Background
Amylin
Chuang, C.-L., & Hay, D. L. (2021) · Springer eBooks · doi:10.1007/978-3-030-57401-7_10021 · Cited by 1 · see citing works
Self-citation
Calcitonin Family Receptors
Garelja, M. L., & Hay, D. L. (2020) · Springer eBooks · doi:10.1007/978-3-030-21573-6_10055-1
Self-citation
Role of Amylin in Thyroid Cancer
Abdalla, M. M. I. (2019) · Journal of Endocrinology and Thyroid Research · doi:10.19080/jetr.2019.04.555631
Calcitonin Family Receptors
Garelja, M. L., & Hay, D. L. (2021) · Springer eBooks · doi:10.1007/978-3-030-57401-7_10055
Self-citation
Amylin
Chuang, C.-L., & Hay, D. L. (2020) · Springer eBooks · doi:10.1007/978-3-030-21573-6_10021-1
Self-citation
Oral delivery of the amylin receptor agonist pramlintide
Sinézia, C., Sisnande, T., Icart, L. P., & Lima, L. M. T. R. (2024) · Peptide Science · doi:10.1002/pep2.24346
Peripheral Modulators of Appetite in Eating Disorders
Procházková, P., Roubalová, R., & Papežová, H. (2024) · Springer eBooks · doi:10.1007/978-3-031-46096-8_113
Coordination Chemistry of Diabetes‐Associated Islet Peptide Hormones
Pi, Y., Jung, H., & Han, J. (2025) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.202500407 · Cited by 1 · see citing works
The calcitonin receptor controls osteophyte formation, but not cartilage degeneration and subchondral bone loss in experimental osteoarthritis
Jiang, S., Xie, W., Ballhause, T. M., Sevecke, J., Augustin, R., Rolvien, T., Maleitzke, T., Baranowsky, A., & Keller, J. (2026) · Bone and Joint Research · doi:10.1302/2046-3758.152.bjr-2025-0025.r1 · Cited by 1 · see citing works
“53 Second, the employed experimental ptOA model is not capable of fully recapitulating the multifactorial pathogenesis of human OA.”
Future Directions in the Medical Treatment of Obesity: A Narrative Review
Bassatne, A., & Rizo, I. M. (2026) · Advances in Therapy · doi:10.1007/s12325-026-03576-6 · Cited by 2 · see citing works
“Amylin is a 37-amino acid hormone co-secreted with insulin from pancreatic beta cells in response to nutrient stimuli [86].”
Influential
Sensory neurons inhibit invadopodia and metastasis via direct CGRP-RAMP1-cAMP signaling to cancer cellsPreprint
Quesada, I. V., Belova, E., Jarrah, A., Mariano, M. C. C., Dahleh, Y., Lima, M. A., Costa, D. B. V., Francescone, R. A., III, Cukierman, E., Hodgson, L., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.17.719233

Novel, Selective Amylin Agonists as Therapeutic Tools to Treat Diabetes
Yule, L. R. (2018) · ResearchSpace (University of Auckland)
Molecular determinants of amylin receptor agonism
Bower, R. (2017) · ResearchSpace (University of Auckland)
Self-citation
Amylin: Pharmacology, Physiology, and Clinical Potential
Hay, D. L., Chen, S., Lutz, T. A., Parkes, D. G., & Roth, J. D. (2015) · Pharmacological Reviews · doi:10.1124/pr.115.010629 · Cited by 400 · see citing works
Self-citation
Structure and biology of amylin
RINK, T. J., Beaumont, K. C., Koda, J. E., & Young, A. W. (1993) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(93)90081-t · Cited by 105 · see citing works
Synthesis and amylin receptor activity of glycomimetics of pramlintide using click chemistry
Yule, L. R., Bower, R. L., Kaur, H., Kowalczyk, R., Hay, D. L., & Brimble, M. A. (2016) · Organic & Biomolecular Chemistry · doi:10.1039/c6ob00850j · Cited by 14 · see citing works
Self-citation

Authors: Bower, R. L., & Hay, D. L.
Affiliations: University of Auckland (NZ)
Corresponding author: Hay, Debbie L
ORCID: Hay, Debbie L
Venue: British Journal of Pharmacology
Publisher: Wiley
Published: 2016-05-18
Volume: 173
Issue: 12
Pages: 1883-1898
ISSN: 0007-1188 (ISSN-L)
1476-5381
DOI: 10.1111/bph.13496
PMC: PMC4882495
OpenAlex: W2335911426
Semantic Scholar: cc043789091801cad46a9f84f624576696d57472
Cited by: 104
References: 90
Citations by year: 2026: 14 · 2025: 8 · 2024: 8 · 2023: 10 · 2022: 6 · 2021: 18 · 2020: 12 · 2019: 9 · 2018: 10 · 2017: 8 · 2016: 1
FWCI: 1.02
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: British Journal of Pharmacology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Treatment and Management
Health Sciences › Medicine › Surgery › Pancreatic function and diabetes
Keywords: amylin, structure-function relationship, pramlintide, amylin receptor, calcitonin receptor, receptor activity-modifying proteins, amylin aggregation, peptide solubility, calcitonin gene-related peptide, hybrid peptides, type 1 diabetes, drug development
MeSH terms: Animals, Humans, Structure-Activity Relationship, Drug Design, Islet Amyloid Polypeptide, Receptors, Islet Amyloid Polypeptide, Amylin Receptor Agonists

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Amylin structure–function relationships and receptor pharmacology: implications for amylin mimetic drug development

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