Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology

Type 2 diabetes as an inflammatory disease

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Macromolecular Crowding and Confinement: Biochemical, Biophysical, and Potential Physiological Consequences

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RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor

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Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes

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Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients.

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A possible role for π‐stacking in the self‐assembly of amyloid fibrils

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Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus

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Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells.

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CD36 coordinates NLRP3 inflammasome activation by facilitating intracellular nucleation of soluble ligands into particulate ligands in sterile inflammation

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Novel insight into streptozotocin-induced diabetic rats from the protein misfolding perspective

Leyva-García, E., Lara‐Martínez, R., Morán, L., Revilla, M., Jiménez‐García, L. F., Oviedo, N., Murata, C., Garrido-Magaña, E. P., Altamirano-Bustamante, N. F., & Altamirano‐Bustamante, M. M. (2017) · Scientific Reports · doi:10.1038/s41598-017-11776-y · Cited by 16

Sub-Toxic Human Amylin Fragment Concentrations Promote the Survival and Proliferation of SH-SY5Y Cells via the Release of VEGF and HspB5 from Endothelial RBE4 Cells

Caruso, G., Fresta, C. G., Lazzarino, G., Distefano, D. A., Parlascino, P., Lunte, S. M., Lazzarino, G., & Caraci, F. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113659 · Cited by 16

Realization of Amyloid-like Aggregation as a Common Cause for Pathogenesis in Diseases

Naskar, S., & Gour, N. (2023) · Life · doi:10.3390/life13071523 · Cited by 13

A Comparison of Amyloid Deposition in Endoscopic and Open Carpal Tunnel Release

Ozdag, Y., Koshinski, J. L., Carry, B. J., Gardner, J. M., Garcia, V. C., Dwyer, C. L., Akoon, A., Klena, J. C., & Grandizio, L. C. (2024) · The Journal Of Hand Surgery · doi:10.1016/j.jhsa.2024.01.002 · Cited by 15

Mechanisms of Transthyretin Inhibition of IAPP Amyloid Formation

Jayaweera, S. W., Surano, S., Pettersson, N., Oskarsson, E., Lettius, L., Gharibyan, A. L., Anan, I., & Olofsson, A. (2021) · Biomolecules · doi:10.3390/biom11030411 · Cited by 15

From Small Peptides to Large Proteins against Alzheimer’sDisease

Picone, P., Sanfilippo, T., Vasto, S., Baldassano, S., Guggino, R., Nuzzo, D., Bulone, D., Biagio, P. L. S., Muscolino, E., Monastero, R., et al. (2022) · Biomolecules · doi:10.3390/biom12101344 · Cited by 16

Evolutionary Adaptation and Amyloid Formation: Does the Reduced Amyloidogenicity and Cytotoxicity of Ursine Amylin Contribute to the Metabolic Adaption of Bears and Polar Bears?

Akter, R., Abedini, A., Ridgway, Z., Zhang, X., Kleinberg, J., Schmidt, A., & Raleigh, D. (2016) · Israel Journal of Chemistry · doi:10.1002/ijch.201600081 · Cited by 13

Transactive DNA Binding Protein 43 Rather Than Other Misfolded Proteins in the Brain is Associated with Islet Amyloid Polypeptide in Pancreas in Aged Subjects with Diabetes Mellitus

Leino, M., Popova, S. N., & Alafuzoff, I. I. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170192 · Cited by 15

Sterol Structure Strongly Modulates Membrane–Islet Amyloid Polypeptide Interactions

Zhang, X., London, E., & Raleigh, D. P. (2018) · Biochemistry · doi:10.1021/acs.biochem.7b01190 · Cited by 15

Determination of the Aggregate Binding Site of Amyloid Protofibrils Using Electron Capture Dissociation Tandem Mass Spectrometry

Lam, Y. P. Y., Wootton, C. A., Hands-Portman, I., Wei, J., Chiu, C. K. C., Romero‐Canelón, I., Lermyte, F., Barrow, M. P., & O’Connor, P. B. (2020) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.9b00053 · Cited by 14

Accumulated or continuous exercise for glycaemic regulation and control: a systematic review with meta-analysis

Shambrook, P., Kingsley, M., Taylor, N. F., & Gordon, B. A. (2018) · BMJ Open Sport & Exercise Medicine · doi:10.1136/bmjsem-2018-000470 · Cited by 15

d -Retro Inverso Amylin and the Stability of Amylin Fibrils

Pandey, P., Nguyen, N. N. M., & Hansmann, U. H. E. (2020) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.0c00523 · Cited by 14

Metastable intermediate during hIAPP aggregation catalyzed by membranes as detected with 2D IR spectroscopy

Dicke, S. S., Maj, M., Fields, C. R., & Zanni, M. T. (2022) · RSC Chemical Biology · doi:10.1039/d2cb00028h · Cited by 13

Kinetic and Conformational Insights into Islet Amyloid Polypeptide Self-Assembly Using a Biarsenical Fluorogenic Probe

Quittot, N., Sebastiao, M., Soultan, A. H., & Bourgault, S. (2018) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.7b00827 · Cited by 13

Structural Modulation of Human Amylin Protofilaments by Naturally Occurring Mutations

Tofoleanu, F., Yuan, Y., Pickard, F. C., Bartłomiej, T., Brooks, B. R., & Buchete, N. (2018) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.7b12083 · Cited by 13

Undercover Toxic Ménage à Trois of Amylin, Copper (II) and Metformin in Human Embryonic Kidney Cells

Congiu, T., Alghrably, M., Emwas, A.-H. M., Jaremko, Ł., Lachowicz, J. I., Piludu, M., Piras, M., Faa, G., Pichiri, G., Jaremko, M., et al. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13060830 · Cited by 13

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 13

ADS-J1 disaggregates semen-derived amyloid fibrils

Li, J., Yang, Z., Liu, H., Qiu, M., Zhang, T., Li, W., Li, Z., Qi, T., Qiu, Y., Li, L., et al. (2019) · Biochemical Journal · doi:10.1042/bcj20180886 · Cited by 12

Fluorescence-based techniques for the detection of the oligomeric status of proteins: implication in amyloidogenic diseases

Mirdha, L., & Chakraborty, H. (2021) · European Biophysics Journal · doi:10.1007/s00249-021-01505-9 · Cited by 12

The Unfolded State of the C-Terminal Domain of L9 Expands at Low but Not at Elevated Temperatures

Stenzoski, N. E., Luan, B., Holehouse, A. S., & Raleigh, D. P. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.07.013 · Cited by 12

Does deamidation of islet amyloid polypeptide accelerate amyloid fibril formation?

Lam, Y. P. Y., Wootton, C. A., Hands-Portman, I., Wei, J., Chiu, C. K. C., Romero‐Canelón, I., Lermyte, F., Barrow, M. P., & O’Connor, P. B. (2018) · Chemical Communications · doi:10.1039/c8cc06675b · Cited by 12

Amyloidogenicity and cytotoxicity of des-Lys-1 human amylin provides insight into amylin self-assembly and highlights the difficulties of defining amyloidogenicity

Lee, K., Zhyvoloup, A., & Raleigh, D. P. (2019) · Protein Engineering Design and Selection · doi:10.1093/protein/gzz036 · Cited by 12

A capillary zone electrophoresis method to investigate the oligomerization of the human Islet Amyloid Polypeptide involved in Type 2 Diabetes

Berardet, C., Kaffy, J., Ongeri, S., & Taverna, M. (2018) · Journal of Chromatography A · doi:10.1016/j.chroma.2018.10.006 · Cited by 11

Inhibition of the Early-Stage Cross-Amyloid Aggregation of Amyloid‑β and IAPP via EGCG: Insights from Molecular Dynamics Simulations

Srivastava, A., Adem, K. A., Shanti, A., Lee, S., Abedrabbo, S. M., & Homouz, D. (2024) · ACS Omega · doi:10.1021/acsomega.4c00500 · Cited by 11

Pathology and Treatments of Alzheimer’s Disease Based on Considering Changes in Brain Energy Metabolism Due to Type 2 Diabetes

Yanai, H., Adachi, H., Hakoshima, M., & Katsuyama, H. (2024) · Molecules · doi:10.3390/molecules29245936 · Cited by 11

Rationally designed cyclic peptides and nanomaterials as ‘next-generation’ anti-amyloid therapeutics

Khairnar, B. D., Jha, A., & Rajwade, J. M. (2023) · Journal of Materials Science · doi:10.1007/s10853-023-08654-6 · Cited by 12

The dye SYPRO orange binds to amylin amyloid fibrils but not pre‐fibrillar intermediates

Wong, A. G., & Raleigh, D. P. (2016) · Protein Science · doi:10.1002/pro.2992 · Cited by 10

Conformation‐specific antibodies against multiple amyloid protofibril species from a single amyloid immunogen

Bonito-Oliva, A., Schedin‐Weiss, S., Younesi, S. S., Tiiman, A., Adura, C., Paknejad, N., Brendel, M., Romin, Y., Parchem, R. J., Graff, C., et al. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14119 · Cited by 10

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

Differential Effects of Aromatic Residues on Amyloid Formation and Cytotoxicity of Human IAPP

Manathunga, L., Zhyvoloup, A., Baghai, A., & Raleigh, D. P. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00267 · Cited by 9

Analysis of Sheep and Goat IAPP Provides Insight into IAPP Amyloidogenicity and Cytotoxicity

Miller, M. E. T., Li, M., Baghai, A., Peetz, V. H., Zhyvoloup, A., & Raleigh, D. P. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00470 · Cited by 9

Imatinib protects against human beta-cell death via inhibition of mitochondrial respiration and activation of AMPK

Elksnis, A., Schiffer, T. A., Palm, F., Wang, Y., Cen, J., Turpaev, K. T., Ngamjariyawat, A., Younis, S., Huang, S., Shen, Y., et al. (2021) · Clinical Science · doi:10.1042/cs20210604 · Cited by 9

Cucurbit[7]uril Inhibits Islet Amyloid Polypeptide Aggregation by Targeting N Terminus Hot Segments and Attenuates Cytotoxicity

Maity, D., Oh, Y., Gremer, L., Hoyer, W., Magzoub, M. M., & Hamilton, A. D. (2022) · Chemistry - A European Journal · doi:10.1002/chem.202200456 · Cited by 9

SORLA mediates endocytic uptake of proIAPP and protects against islet amyloid deposition

Shih, A. Z. L., Chen, Y., Speckmann, T., Søndergaard, E., Schürmann, A., Verchere, C. B., & Willnow, T. E. (2022) · Molecular Metabolism · doi:10.1016/j.molmet.2022.101585 · Cited by 11

Nanoparticles and Nanocolloidal Carbon: Will They Be the Next Antidiabetic Class That Targets Fibrillation and Aggregation of Human Islet Amyloid Polypeptide in Type 2 Diabetes?

Szunerits, S., Abderrahmani, A., & Boukherroub, R. (2022) · Accounts of Chemical Research · doi:10.1021/acs.accounts.2c00415 · Cited by 9

Polyphenolic Gallotannins 1,3,6-Tri-O-galloyl-β- d -glucose and Corilagin Attenuate IAPP Amyloid Formation and Cytotoxicity by Primarily Targeting Secondary Nucleation

Khalifa, J., Sulaimon, R., Côté‐Cyr, M., Nguyen, P. T., Peslherbe, G. H., Bourgault, S., & Gaudreault, R. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00139 · Cited by 8

Assessing the role of osmolytes on the conformational harmony of islet amyloid polypeptide

Kumari, A., Sharma, R., Somvanshi, P., & Grover, A. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.08.104 · Cited by 9

Protein-conformational diseases in childhood: Naturally-occurring hIAPP amyloid-oligomers and early β-cell damage in obesity and diabetes

Altamirano-Bustamante, N. F., Garrido-Magaña, E. P., Morán, E., Calderón, A., Pastén-Hidalgo, K., Castillo‐Rodríguez, R. A., Rojas, G., Lara‐Martínez, R., Leyva-García, E., Larralde-Laborde, M., et al. (2020) · PLoS ONE · doi:10.1371/journal.pone.0237667 · Cited by 8

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

Bridging Pancreatic Amyloidosis and Neurodegeneration: The Emerging Role of Amylin in Diabetic Dementia

Shome, G., Mondal, R., Deb, S., Roy, J., Mandal, A. K., & Benito‐León, J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26115021 · Cited by 8

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

Effect of Post-Translational Amidation on Islet Amyloid Polypeptide Conformational Ensemble: Implications for Its Aggregation Early Steps

Tran, L., & Ha‐Duong, T. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17111896 · Cited by 8

Site-Specific Alkylation of the Islet Amyloid Polypeptide Accelerates Self-Assembly and Potentiates Perturbation of Lipid Membranes

Babych, M., Nguyen, P. T., Côté‐Cyr, M., Kihal, N., Quittot, N., Golizeh, M., Sleno, L., & Bourgault, S. (2021) · Biochemistry · doi:10.1021/acs.biochem.1c00308 · Cited by 9

Current amyloid inhibitors: Therapeutic applications and nanomaterial-based innovations

López-García, P., Tejero-Ojeda, M. M., Vaquero, M. E., & Carrión‐Vázquez, M. (2025) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2025.102734 · Cited by 8

Chemical synthesis uncovers the significant impact of natural glycosylation on islet amyloid polypeptide aggregation

Li, Y., Liu, W., Wang, R., Liu, D., Li, X., Zhang, C., Gong, J., Song, Z., Zhang, Y., & Tan, Z. (2025) · Science Advances · doi:10.1126/sciadv.adx8201 · Cited by 7

Protein Aggregation and Self Assembly in Health and Disease

Basak, A., & Basak, S. (2021) · Current Proteomics · doi:10.2174/1570164618666210223160742 · Cited by 7

Resveratrol protects pancreatic beta cell and hippocampal cells from the aggregate-prone capacity of hIAPP

González-Blanco, C., Lockwood, Á. C., Jiménez, B., Iglesias-Fortes, S., Marqués, P., García, G., García-Aguilar, A., Benito, M., & Guillén, C. (2024) · Scientific Reports · doi:10.1038/s41598-024-78967-2 · Cited by 7

Lipids determine the toxicity of human islet polypeptide aggregates in vivo

Sitton, J., Pickett, D. N., Rodriguez, A., & Kurouski, D. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.108029 · Cited by 8

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

A GLP‑1 receptor agonist attenuates human islet amyloid polypeptide‑induced autophagy and apoptosis in MIN6 cells

Chen, X., Huang, T., Shi, Y., Wang, L., Li, W., Shen, F., & Gu, X. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.9741 · Cited by 7

The triphenylmethane dye brilliant blue G is only moderately effective at inhibiting amyloid formation by human amylin or at disaggregating amylin amyloid fibrils, but interferes with amyloid assays; Implications for inhibitor design

Akter, R., Zhyvoloup, A., Zheng, B., Bhatia, S. R., & Raleigh, D. P. (2019) · PLoS ONE · doi:10.1371/journal.pone.0219130 · Cited by 7

Connecting Alzheimer’s Disease With Diabetes Mellitus Through Amyloidogenic Evolvability

Ho, G. J., Takamatsu, Y., Wada, R., Sugama, S., Waragai, M., Takenouchi, T., Masliah, E., & Hashimoto, M. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.576192 · Cited by 7

Tyrosine 12 of human calcitonin modulates its amyloid formation, membrane binding, and bioactivity

Hsieh, I.-C., Chen, T.-W., Chuang, Y., Lai, Y., & Tu, L. (2022) · Biochimie · doi:10.1016/j.biochi.2022.02.007 · Cited by 7

Mechanistic insight into functionally different human islet polypeptide (hIAPP) amyloid: the intrinsic role of the C-terminal structural motifs

Sarkar, D., Maity, N. C., Shome, G., Varnava, K. G., Sarojini, V., Vivekanandan, S., Sahoo, N., Kumar, S., Mandal, A. K., Biswas, R., et al. (2022) · Physical Chemistry Chemical Physics · doi:10.1039/d2cp01650h · Cited by 7

Urolithin B: Two-way attack on IAPP proteotoxicity with implications for diabetes

Raimundo, A., Ferreira, S., Pobre, V., Lopes‐da‐Silva, M., Brito, J. A., dos Santos, D. J. V. A., Saraiva, N., dos Santos, C. N., & Menezes, R. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.1008418 · Cited by 7

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

The Fluorescent Dye 1,6-Diphenyl-1,3,5-hexatriene Binds to Amyloid Fibrils Formed by Human Amylin and Provides a New Probe of Amylin Amyloid Kinetics

Li, M., Manathunga, L., London, E., & Raleigh, D. P. (2021) · Biochemistry · doi:10.1021/acs.biochem.1c00328 · Cited by 7

Peptidylglycine alpha-amidating monooxygenase is important in mice for beta-cell cilia formation and insulin secretion but promotes diabetes risk through beta-cell independent mechanisms

Chen, Y., Bäck, N., Zhen, J., Xiong, L., Komba, M., Gloyn, A. L., MacDonald, P. E., Mains, R. E., Eipper, B. A., & Verchere, C. B. (2025) · Molecular Metabolism · doi:10.1016/j.molmet.2025.102123 · Cited by 9

Exploring the Propensities of Fluorescent Carbazole Analogs toward the Inhibition of Amyloid Aggregation in Type 2 Diabetes: An Experimental and Theoretical Endeavor

Mallick, T., Karmakar, A., Mukhuty, A., Fouzder, C., Mandal, J., Mondal, S., Pramanik, A., Kundu, R., & Begum, N. A. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c06161 · Cited by 6

De novo amyloid peptides with subtle sequence variations differ in their self-assembly and nanomechanical properties

Abernathy, H. G., Saha, J., Kemp, L. K., Wadhwani, P., Clemons, T. D., Morgan, S. E., & Rangachari, V. (2023) · Soft Matter · doi:10.1039/d3sm00604b · Cited by 6

Heterologous Expression of Immature Forms of Human Islet Amyloid Polypeptide in Yeast Triggers Intracellular Aggregation and Cytotoxicity

Raimundo, A., Ferreira, S., Farrim, M. I. D. J. D., dos Santos, C. N., & Menezes, R. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.02035 · Cited by 10

Quantitative, High-Throughput Assays for Proteolytic Degradation of Amylin

Suire, C. N., Brizuela, M. K., & Leissring, M. A. (2020) · Methods and Protocols · doi:10.3390/mps3040081 · Cited by 6

Molecular mechanics and quantum chemical calculations unveil the combating effect of baicalein on human islet amyloid polypeptide aggregates

Srinivasan, E., Ravikumar, S., Venkataramanan, S., Purohit, R., & Rajasekaran, R. (2019) · Molecular Simulation · doi:10.1080/08927022.2019.1660778 · Cited by 6

Protein aggregates and biomolecular condensates: implications for human health and disease

Navalkar, A., Arunagiri, A., Kee, T., Panchal, K., & Dick, K. (2025) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2025.1719678 · Cited by 5

On the plasticity of amyloid formation: The impact of destabilizing small to large substitutions on islet amyloid polypeptide amyloid formation

Manathunga, L., Akter, R., Zhyvoloup, A., Simmerling, C. L., & Raleigh, D. P. (2022) · Protein Science · doi:10.1002/pro.4539 · Cited by 4

Non-fibril form but not fibril form of human islet amyloid polypeptide 8–20 changes brain functions in mice

Suginoma, H., Owada, R., Katano-Toki, A., Mori, A., Fujioka, J., & Nakamura, K. (2024) · PLoS ONE · doi:10.1371/journal.pone.0296750 · Cited by 5

Composition and Conformation of Hetero‐ versus Homo‐Fluorinated Triazolamers Influence their Activity on Islet Amyloid Polypeptide Aggregation

Arenas, J. L., Lesma, J., Ha‐Duong, T., Sahoo, B. R., Ramamoorthy, A., Tonali, N., Soulier, J. L., Halgand, F., Giraud, F., Crousse, B., et al. (2024) · Chemistry - A European Journal · doi:10.1002/chem.202303887 · Cited by 5

Inhibitory effect of saffron components on hIAPP fibrils formation; a molecular dynamics simulation study

Kordzadeh, A., Minaeian, M., & A., A. R. S. (2024) · Computational and Theoretical Chemistry · doi:10.1016/j.comptc.2024.114481 · Cited by 5

Computational and Experimental Approaches to Design Inhibitors of Amylin Aggregation

Kumar, A. P., Lee, S., & Lukman, S. (2019) · Current Drug Targets · doi:10.2174/1389450120666190719164316 · Cited by 5

Differential effects of serine side chain interactions in amyloid formation by islet amyloid polypeptide

Akter, R., Zou, J., & Raleigh, D. P. (2019) · Protein Science · doi:10.1002/pro.3782 · Cited by 6

Analysis of Prairie Vole Amylin Reveals the Importance of the N-terminus and Residue-22 in Amyloidogenicity and Cytotoxicity

Lee, K.-H., Noh, D., Zhyvoloup, A., & Raleigh, D. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00952 · Cited by 5

Helix Dipole and Membrane Electrostatics Delineate Conformational Transitions in the Self-Assembly of Amyloidogenic Peptides

Zheng, Q., Carty, S., & Lazo, N. D. (2020) · Langmuir · doi:10.1021/acs.langmuir.0c00723 · Cited by 5

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

Neuroinflammation induced by amyloid-forming pancreatic amylin: Rationale for a mechanistic hypothesis

Leibold, N. S., & Despa, F. (2024) · Biophysical Chemistry · doi:10.1016/j.bpc.2024.107252 · Cited by 5

A Survey and Guide to the Development of Fatty Acid‐derivatized Peptide Therapeutics

Jacobsen, M. T., Poulsen, C., Kopp, K. L., Olsen, J., & Cox, N. (2025) · Peptide Science · doi:10.1002/9781119824701.ch07 · Cited by 5

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 5

Easy Production of “Difficult Peptides” Using Cell‐Free Protein Synthesis and a New Methionine Analogue as a Latent Peptide Cleavage Site

Fankhauser, D., Alissandratos, A., Liutkus, M., & Easton, C. J. (2021) · Chemistry - A European Journal · doi:10.1002/chem.202103161 · Cited by 4

Assessment of Amyloid Forming Tendency of Peptide Sequences from Amyloid Beta and Tau Proteins Using Force-Field, Semi-Empirical, and Density Functional Theory Calculations

Muvva, C., Murugan, N. A., & Subramanian, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22063244 · Cited by 4

Molecular basis of the anchoring and stabilization of human islet amyloid polypeptide in lipid hydroperoxidized bilayers

Espinosa, Y. R., Valderrama, D. I. B., Carlevaro, C. M., & Llanos, E. J. (2022) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2022.130200 · Cited by 4

Is islet amyloid polypeptide indeed expressed in the human brain?

Libard, S., & Alafuzoff, I. I. (2023) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12917 · Cited by 4

Encapsulation of Ciprofloxacin into a Cyclodextrin Polymer Matrix: The Complex Formation with Human Serum Albumin and In Vitro Studies

Скуредина, А. А., Скуредина, А. А., Belogurova, N. G., & Kudryashova, E. V. (2023) · Chemistry · doi:10.3390/chemistry5030132 · Cited by 4

Exploring the locking stage of NFGAILS amyloid fibrillation via transition manifold analysis

Bittracher, A., Moschner, J., Koksch, B., Netz, R. R., & Schütte, C. (2021) · The European Physical Journal B · doi:10.1140/epjb/s10051-021-00200-0 · Cited by 4

Bifunctional nanodisc platforms for studies on self-assembly and amyloid fibrillation

Sahoo, B. R., Watanabe‐Nakayama, T., Suladze, S., Anantharamaiah, G. M., Reif, B., & Ramamoorthy, A. (2025) · Chemical Communications · doi:10.1039/d5cc00972c · Cited by 3

Brain insulin resistance as a driver of proteinopathy in neurodegeneration: from cell-type-specific mechanisms to targeted therapeutics

Xiang, M., Cao, S.-Y., Sun, X.-H., Hu, J.-W., Lv, M., Li, J., & Li, W. (2026) · Translational Neurodegeneration · doi:10.1186/s40035-026-00573-1 · Cited by 3

Metabolic perturbations associated with hIAPP-induced insulin resistance in skeletal muscles: Implications to the development of type 2 diabetes

Naik, A. R., Save, S. N., Sahoo, S. S., Yadav, S. S., Kumar, A., Chugh, J., & Sharma, S. (2024) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2024.106665 · Cited by 3

Effect of a SARS-CoV-2 Protein Fragment on the Amyloidogenic Propensity of Human Islet Amyloid Polypeptide

Bilog, M., Cersosimo, J., Vigil, I., Desamero, R. Z. B., & Profit, A. A. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00473 · Cited by 3

Amylin is incorporated into extracellular vesicles in an ESCRT-dependent manner and regulates senescence

Iglesias-Fortes, S., Lockwood, A. C., González-Blanco, C., Lozano, D., García-Aguilar, A., Palomino, O. M., García, G., Fernández‐Millán, E., Benito, M., & Guillén, C. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2025.167699 · Cited by 3

Modulation of hIAPP Fibrillation by Rationally Designed Hexapeptides Revealed by Molecular Dynamics and Experimental Investigations

Rani, D., Priyadarshi, N., Singhal, N. K., & Goyal, B. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00269 · Cited by 3

Obesity-Dependent Accumulation of Titanium in the Pancreas of Type 2 Diabetic Donors

Heller, A., Coffman, S. S., & Friedman, K. A. (2019) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.8b00304 · Cited by 3

Amyloid-Like Peptide Aggregates

Kokotidou, C., Tamamis, P., & Mitraki, A. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781839161148-00217 · Cited by 3

Microcanonical insights into the physicochemical stability of the coformulation of insulin with amylin analogues

Frigori, R. B., & Rodrigues, F. R. M. (2021) · Journal of Molecular Modeling · doi:10.1007/s00894-020-04617-9 · Cited by 3

Aggregation characteristics of non-aromatic polar amino acids and its association to amyloidsPreprint

Gour, N., Jaiswal, A., Patel, M., Revi, N., Rengan, A. K., & Verma, S. K. (2023) · ChemRxiv · doi:10.26434/chemrxiv-2023-9lk05-v3 · Cited by 3

Cross-domain binding of anti-fibrillation peptide TNGQ to islet amyloid polypeptide provides cytoprotective effects in giant unilamellar vesicles and pancreatic β-cells

Abioye, R. O., Yiridoe, M. S., Wang, C., Avis, T. J., Ahmed, T. A., Hammami, R., & Udenigwe, C. C. (2024) · Food & Function · doi:10.1039/d4fo03322a · Cited by 2

Unraveling the Role of Functional Amyloids and Amyloid Peptides in Disease Detection

Kumar, P. R., & Sarkar, N. (2025) · Protein and Peptide Letters · doi:10.2174/0109298665368109250419175111 · Cited by 2

Mechanistic insights into the inhibition of hIAPP fibrillation by amyloidogenic core-derived peptide NFGAILSS using computer simulations

Mehta, T., & Goyal, B. (2026) · Physical Chemistry Chemical Physics · doi:10.1039/d5cp03150h · Cited by 2

Impact of Ca2+ on membrane catalyzed IAPP amyloid formation and IAPP induced vesicle leakage

Li, M., Zhang, X., London, E., & Raleigh, D. P. (2023) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2023.184161 · Cited by 2

TPE conjugated islet amyloid polypeptide probe for detection of peptide oligomers

Tsai, H.-C., Huang, C.-H., & Tu, L. (2023) · Biophysical Chemistry · doi:10.1016/j.bpc.2023.107129 · Cited by 2

Experimental and computational investigation of the effect of Hsc70 structural variants on inhibiting amylin aggregation

Châari, A., Saikia, N., Paul, P., Yousef, M. S., Ding, F., & Ladjimi, M. M. (2024) · Biophysical Chemistry · doi:10.1016/j.bpc.2024.107235 · Cited by 2

Effect of Pressure on the Conformational Landscape of Human γD-Crystallin from Replica Exchange Molecular Dynamics Simulations

Kacirani, A., Uralcan, B., Domingues, T. S., & Haji‐Akbari, A. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.4c00178 · Cited by 3

Matching model with mechanism: Appropriate rodent models for studying various aspects of diabetes pathophysiology

Gatward, L. F. D., & King, A. (2024) · Methods in cell biology · doi:10.1016/bs.mcb.2024.05.003 · Cited by 3

Islet amyloid: From fundamental biophysics to mechanisms of cytotoxicity

Cao, P., Marek, P., Noor, H., Patsalo, V., Tu, L., Wang, H., Abedini, A., & Raleigh, D. P. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.046 · Cited by 178

Islet amyloid toxicity: From genesis to counteracting mechanisms

Marmentini, C., Branco, R. C. S., Boschero, A. C., & Kurauti, M. A. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30600 · Cited by 19

Recent progress of islet amyloid polypeptide

Huang, K. (2010) · Shengming kexue · Cited by 1

Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology

Cao, P., Abedini, A., & Raleigh, D. P. (2012) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2012.11.003 · Cited by 119

George Scatchard, John G. Kirkwood, and the electrical interactions of amino acids and proteins

Edsall, J. T. (1982) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(82)90189-x · Cited by 4