Islet amyloid polypeptide toxicity and membrane interactions

Protein Misfolding, Functional Amyloid, and Human Disease

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Calcium Dysregulation and Membrane Disruption as a Ubiquitous Neurotoxic Mechanism of Soluble Amyloid Oligomers*♦

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Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus

Westermark, P., Andersson, A., & Westermark, G. T. (2011) · Physiological Reviews · doi:10.1152/physrev.00042.2009 · Cited by 1,044

Diabetes Mellitus and the β Cell: The Last Ten Years

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Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases

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Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus

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The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles.

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Islet amyloid, increased A-cells, reduced B-cells and exocrine fibrosis: quantitative changes in the pancreas in type 2 diabetes.

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Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane

Engel, M. F., Khemtemourian, L., Kleijer, C. C., Meeldijk, H. J. D., Jacobs, J., Verkleij, A., de Kruijff, B., Killian, J., & Höppener, J. (2008) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0708354105 · Cited by 465

Evidence of Cosecretion of Islet Amyloid Polypeptide and Insulin by β-Cells

Kahn, S. E., D'Alessio, D. A., Schwartz, M. W., Fujimoto, W. Y., Ensinck, J. W., Taborsky, G. J., & Porte, D. (1990) · Diabetes · doi:10.2337/diab.39.5.634 · Cited by 454

Interspecies Variation Affects Islet Amyloid Polypeptide Membrane Binding

Sanders, H. M., Chalyavi, F., Fields, C. R., Kostelic, M. M., Li, M., Raleigh, D. P., Zanni, M. T., & Marty, M. T. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00005 · Cited by 7

Teaching an old scaffold new recognition tricks: oligopyrrolamide antagonists of IAPP aggregation

Kumar, S., Vogel, M. C., & Hamilton, A. D. (2017) · Organic & Biomolecular Chemistry · doi:10.1039/c7ob02910a · Cited by 7

Role of lysine residue of islet amyloid polypeptide in fibril formation, membrane binding, and inhibitor binding

Wu, M., Chan, A.-C., & Tu, L. (2020) · Biochimie · doi:10.1016/j.biochi.2020.08.012 · Cited by 7

Interplay between human islet amyloid polypeptide aggregates and micro-heterogeneous membranes

Tan, Q., Liu, H., Duan, M., & Huo, S. (2021) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2021.183691 · Cited by 7

New Human Islet Amyloid Polypeptide Fragments Susceptible to Aggregation

Rożniakowski, K., Fraczyk, A., Gałęcki, K., Wietrzyk, J., Filip‐Psurska, B., Frączyk, J., Kaminski, Z. J., & Kolesińska, B. (2020) · Chemistry & Biodiversity · doi:10.1002/cbdv.202000501 · Cited by 7

Exploring interactions between lipids and amyloid-forming proteins: A review on applying fluorescence and NMR techniques

Chang, Z., Deng, J., Zhao, W., & Yang, J. (2021) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2021.105062 · Cited by 7

Mammals that can develop type 2 diabetes have a similarly structured β-sheet amyloid oligomer

LeMasters, B. E., Fields, C. R., Lomont, J. P., Chalyavi, F., Rich, K. L., Stapleton, D. S., Dicke, S. S., Keller, M. P., Attie, A., & Zanni, M. T. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2530570123 · Cited by 5

Modulation of Lipid Dynamics in the β-Amyloid Aggregates Induced Membrane Fragmentation

Qiang, W., Kengewerere, M. K., & Kenyaga, J. M. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.4c02119 · Cited by 6

The Molecular Physiopathogenesis of Islet Amyloidosis

Bhowmick, D. C., Singh, S., Trikha, S., & Jeremic, A. M. (2017) · Handbook of experimental pharmacology · doi:10.1007/164_2017_62 · Cited by 8

Intravenous immunoglobulin improves glucose control and β-cell function in human IAPP transgenic mice by attenuating islet inflammation and reducing IAPP oligomers

Zhang, Y., Yu, X., Zhu, J., Liu, S., Liu, X., Dong, Q.-X., Chai, J.-Q., & Liu, R. (2017) · International Immunopharmacology · doi:10.1016/j.intimp.2017.11.012 · Cited by 6

O-glycosylated peptides curtail the aggregation and toxicity of human islet amyloid polypeptide

Zhang, Q., Mei, X., Li, Y., Wang, Z., Li, A., Liu, D., Kumar, S., Kong, D., Hamilton, A. D., & Zhang, C. (2025) · Communications Biology · doi:10.1038/s42003-025-08516-8 · Cited by 5

Nitration of Tyr37 alters the aggregation pathway of hIAPP and enhances its cytotoxicity

Wang, Z., Wei, J., Zhang, X., Ji, H., Fu, S., Gao, Z., & Li, H. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.138367 · Cited by 5

Deuterium trafficking, mitochondrial dysfunction, copper homeostasis, and neurodegenerative disease

Seneff, S., & Kyriakopoulos, A. M. (2025) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2025.1639327 · Cited by 5

Development of a novel fluorescence assay for studying lipid bilayer perturbation induced by amyloidogenic peptides using cell plasma membrane vesicles

Sebastiao, M., Babych, M., Quittot, N., Kumar, K., Arnold, A. A., Marcotte, I., & Bourgault, S. (2023) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2022.184118 · 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

Delineating the Role of Helical Intermediates in Natively Unfolded Polypeptide Amyloid Assembly and Cytotoxicity

Carufel, C. A. D., Quittot, N., Nguyen, P. T., & Bourgault, S. (2015) · Angewandte Chemie · doi:10.1002/ange.201507092 · Cited by 5

Molecular dynamics study of water channels in natural and synthetic amyloid-β fibrils

Natesh, S. R., Hummels, A. R., Sachleben, J. R., Sosnick, T. R., Freed, K. F., Douglas, J. F., Meredith, S. C., & Haddadian, E. J. (2021) · The Journal of Chemical Physics · doi:10.1063/5.0049250 · Cited by 4

Islet amyloid polypeptide tagged with green fluorescent protein localises to mitochondria and forms filamentous aggregates in Caenorhabditis elegans

Akdag, M., van Schijndel, V., & Sinnige, T. (2024) · Biophysical Chemistry · doi:10.1016/j.bpc.2024.107180 · Cited by 4

The mechanism of phosphatidylcholine‐induced interference of PAP (248‐286) aggregation

Kumar, V., Gour, S., Verma, N., Kumar, S., Gadhave, K., Mishra, P. M., Goyal, P., Pandey, J., Giri, R., & Yadav, J. K. (2019) · Journal of Peptide Science · doi:10.1002/psc.3152 · 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

Protein Fibrillar Nanopolymers: Molecular-Level Insights into Their Structural, Physical and Mechanical Properties

Trusova, V. M. (2015) · Biophysical Reviews and Letters · doi:10.1142/s1793048015300029 · Cited by 4

Growth, Polymorphism, and Spatially Controlled Surface Immobilization of Biotinylated Variants of IAPP21–27 Fibrils

John, T., Bandak, J., Sarveson, N., Hackl, C., Risselada, H. J., Prager, A., Elsner, C., & Abel, B. (2019) · Biomacromolecules · doi:10.1021/acs.biomac.9b01466 · Cited by 4

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

Probing the relationships between self-assembly and the antimicrobial activity of amyloidogenic peptides: The islet amyloid polypeptide as a case study

Nguyen, V., Côté‐Cyr, M., Finatto, A. N., Babych, M., Nguyen, P. T., Sebastiao, M., & Bourgault, S. (2025) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2025.130812 · Cited by 3

In Vitro Studies of Membrane Permeability Induced by Amyloidogenic Polypeptides Using Large Unilamellar Vesicles

Cao, P., & Raleigh, D. P. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2978-8_18 · Cited by 4

Differential effects of SARS-CoV-2 amyloidogenic segments on the aggregation and toxicity of human islet amyloid polypeptide within membrane environments

Zhang, J., Mesias, V. S. D., Chesney, A. D., Anand, V. K., Feng, X., Hsing, I., Hansmann, U. H. E., & Huang, J. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.137930 · Cited by 3

Coexisting Ordered and Disordered Membrane Phases Have Distinct Modes of Interaction with Disease-Associated Oligomers

Gupta, A., Dey, S., Bhowmik, D., & Maiti, S. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c09421 · Cited by 3

Amyloidogenic SARS-CoV-2 Spike Protein-Derived Peptides Form Oligomers and Selectively Damage Lipid Membranes

Adewoye, A., Ezeigbo, E., Vo, Q., & Legleiter, J. A. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00290 · 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

Fluorescence Resonance Energy Transfer to Detect Plasma Membrane Perturbations in Giant Plasma Membrane Vesicles

Sebastiao, M., Quittot, N., Marcotte, I., & Bourgault, S. (2023) · BIO-PROTOCOL · doi:10.21769/bioprotoc.4838 · Cited by 2

Detergent-induced aggregation of an amyloidogenic intrinsically disordered protein

Arya, S., Dogra, P., Jain, N., & Mukhopadhyay, S. (2017) · Journal of Chemical Sciences · doi:10.1007/s12039-017-1386-z · Cited by 2

Imaging Flow Cytometry Illuminates New Dimensions of Amyloid Peptide-Membrane Interactions

Israeli, R., Kolusheva, S., Hadad, U., & Jelinek, R. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.01.018 · Cited by 2

Treatment options for Alzheimer’s Disease: An overview of the amyloid, tau, and alternate hypotheses

Eroltu, K. (2023) · Journal of High School Science · doi:10.64336/001c.89250 · Cited by 1

Amylin at the crossroads of type 2 diabetes and neurodegenerative diseases

Castillo, I. L. D., Garcia-Martin, J., Gutiérrez, A., & Moreno‐González, I. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103226 · Cited by 1

Aβ Fibrils Can Act as Aqueous Pores: a Molecular Dynamics StudyPreprint

Natesh, S., Sachleben, J. R., Sosnick, T. R., Freed, K. F., Meredith, S. C., & Haddadian, E. J. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/418137 · Cited by 1

Heterogeneous Amyloid β-Sheet Polymorphs Identified on Hydrogen Bond Promoting Surfaces Using 2D SFG Spectroscopy

Ho, J.-J., Ghosh, A., Zhang, T. O., & Zanni, M. T. (2018) · The Journal of Physical Chemistry C · doi:10.1021/acs.jpcc.7b11934

Mechanism and Development of Peptide-Based Inhibitors to Human Islet Amyloid Polypeptide (hIAPP) Self-Assembly

Vedad, J. (2018) · CUNY Academic Works (City University of New York)

O papel de lipídios oxidados e surfactantes como promotores de agregados proteicos tipo amilóide

Campos, G. S. M. (2019) · doi:10.11606/t.43.2019.tde-15102019-170824

EXPLORATORY STUDY OF CORPORATE SOCIAL RESPONSIBILITY: BLOGS AS A COMMUNICATION TOOL TO ENHANCE COMPANY- STAKEHOLDERS RELATIONSHIPS

Pallez, M. A. (2013) · Americanae (AECID Library)

Functional and structural characterization of membrane-binding proteins using NMR

Nishimura, K., & Tanio, M. (2022) · Annual reports on NMR spectroscopy · doi:10.1016/bs.arnmr.2021.06.001

Intrinsically disordered proteins share a common molecular mechanism in membranes damages: Lipid-chaperone hypothesis

Rosa, C. L. (2020) · doi:10.1021/scimeetings.0c00244

Fractal nature of benzene stacking interactions

Jovanovic, N. M., Etinski, M., & Stanković, I. M. (2023) · Journal of Molecular Modeling · doi:10.1007/s00894-023-05689-z

The Effects of Naturally Occurring Phenols on Amyloid Fibrils from Insulin in the Liquid Phase Using Atomic Force Microscopy

Dasani, D. B., Nghiem, T. P., Facteau, K. A., Pollock, C. A., Strain, M., Zuchowski, G. E., & Moriarty, D. F. (2025) · Natural Product Communications · doi:10.1177/1934578x241306603

Développement de techniques physiques et chimiques pour l’étude et l’inhibition de l’oligomérisation et de l’agrégation de IAPP : intérêt dans le diabète de type II

Berardet, C. (2018) · theses.fr (ABES) · doi:10.70675/30f4f4ebze047z461bzb24cz3dd0c58274ab

Decongested 2D IR Spectra Reveal N-Terminal Helices in Amyloid Oligomers Associated with Type 2 Diabetes

Shivani, S. T., Maurais, J., LeMasters, B. E., Esterly, H. J., & Zanni, M. T. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c16754

Inhibition of hIAPP amyloid aggregation by the polyherbal formulation NAMIG-5: a bench-to-bedside translational study

Nama, P., Roy, D., Bhunia, P. K., Biswas, K., Suladze, S., Reif, B., Biswas, R., Mroue, K., Ghosh, D., Harikishore, A., et al. (2026) · Biophysical Chemistry · doi:10.1016/j.bpc.2026.107720

Islet amyloid polypeptide‐induced membrane leakage involves uptake of lipids by forming amyloid fibers

Sparr, E., Engel, M. F. M., Sakharov, D. V., Sprong, M., Jacobs, J., KRUIJFF, B. D., Höppener, J. W. M., & Killian, J. A. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.09.075 · Cited by 257

Membrane permeabilization by Islet Amyloid Polypeptide

Engel, M. F. M. (2009) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2009.03.008 · Cited by 129

Islet Amyloid Polypeptide Membrane Interactions: Effects of Membrane Composition

Zhang, X., Clair, J. R. S., London, E., & Raleigh, D. P. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b01016 · Cited by 123

Membrane interaction of islet amyloid polypeptide

Jayasinghe, S. A., & Langen, R. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.01.022 · Cited by 181

In Vitro Studies of Membrane Permeability Induced by Amyloidogenic Polypeptides Using Large Unilamellar Vesicles

Cao, P., & Raleigh, D. P. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2978-8_18 · Cited by 4