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Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes
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    Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes
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    Chemical Reviews

    Cite this: Chem. Rev. 2021, 121, 3, 1845–1893
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    https://doi.org/10.1021/acs.chemrev.0c00981
    Published January 11, 2021
    Copyright © 2021 American Chemical Society

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    The possible link between hIAPP accumulation and β-cell death in diabetic patients has inspired numerous studies focusing on amyloid structures and aggregation pathways of this hormone. Recent studies have reported on the importance of early oligomeric intermediates, the many roles of their interactions with lipid membrane, pH, insulin, and zinc on the mechanism of aggregation of hIAPP. The challenges posed by the transient nature of amyloid oligomers, their structural heterogeneity, and the complex nature of their interaction with lipid membranes have resulted in the development of a wide range of biophysical and chemical approaches to characterize the aggregation process. While the cellular processes and factors activating hIAPP-mediated cytotoxicity are still not clear, it has recently been suggested that its impaired turnover and cellular processing by proteasome and autophagy may contribute significantly toward toxic hIAPP accumulation and, eventually, β-cell death. Therefore, studies focusing on the restoration of hIAPP proteostasis may represent a promising arena for the design of effective therapies. In this review we discuss the current knowledge of the structures and pathology associated with hIAPP self-assembly and point out the opportunities for therapy that a detailed biochemical, biophysical, and cellular understanding of its aggregation may unveil.

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    2. Alexander I. P. Taylor, Yong Xu, Martin Wilkinson, Pijush Chakraborty, Alice Brinkworth, Leon F. Willis, Anastasia Zhuravleva, Neil A. Ranson, Richard Foster, Sheena E. Radford. Kinetic Steering of Amyloid Formation and Polymorphism by Canagliflozin, a Type-2 Diabetes Drug. Journal of the American Chemical Society 2025, Article ASAP.
    3. Abid Ali, Aidan P. Holman, Axell Rodriguez, Kiryl Zhaliazka, Luke Osborne, Dmitry Kurouski. Large Unilamellar Vesicles of Phosphatidic Acid Reduce the Toxicity of α-Synuclein Fibrils. Molecular Pharmaceutics 2024, 21 (3) , 1334-1341. https://doi.org/10.1021/acs.molpharmaceut.3c01012
    4. Chenghui Shi, Julia Kaffy, Tâp Ha-Duong, Jean-François Gallard, Alain Pruvost, Aloise Mabondzo, Lidia Ciccone, Sandrine Ongeri, Nicolo Tonali. Proteolytically Stable Diaza-Peptide Foldamers Mimic Helical Hot Spots of Protein–Protein Interactions and Act as Natural Chaperones. Journal of Medicinal Chemistry 2023, 66 (17) , 12005-12017. https://doi.org/10.1021/acs.jmedchem.3c00611
    5. Rituparna Roy, Sandip Paul. Exploring the Curvature-Dependence of Boron Nitride Nanoparticles on the Inhibition of hIAPP Aggregation. The Journal of Physical Chemistry B 2023, 127 (35) , 7558-7570. https://doi.org/10.1021/acs.jpcb.3c02689
    6. Samuel D. McCalpin, Malitha C. Dickwella Widanage, Riqiang Fu, Ayyalusamy Ramamoorthy. On-Pathway Oligomer of Human Islet Amyloid Polypeptide Induced and Stabilized by Mechanical Rotation during Magic Angle Spinning Nuclear Magnetic Resonance. The Journal of Physical Chemistry Letters 2023, 14 (34) , 7644-7649. https://doi.org/10.1021/acs.jpclett.3c02009
    7. Phuong. H. Nguyen, Fabio Sterpone, Philippe Derreumaux. Self-Assembly of Amyloid-Beta (Aβ) Peptides from Solution to Near In Vivo Conditions. The Journal of Physical Chemistry B 2022, 126 (49) , 10317-10326. https://doi.org/10.1021/acs.jpcb.2c06375
    8. Asra Nasir Khan, Faisal Nabi, Mohammad Rehan Ajmal, Syed Moasfar Ali, Fahad M. Almutairi, Adel I. Alalawy, Rizwan Hasan Khan. Moxifloxacin Disrupts and Attenuates Aβ42 Fibril and Oligomer Formation: Plausibly Repositioning an Antibiotic as Therapeutic against Alzheimer’s Disease. ACS Chemical Neuroscience 2022, 13 (16) , 2529-2539. https://doi.org/10.1021/acschemneuro.2c00371
    9. Barend O. W. Elenbaas, Lucie Khemtemourian, J. Antoinette Killian, Tessa Sinnige. Membrane-Catalyzed Aggregation of Islet Amyloid Polypeptide Is Dominated by Secondary Nucleation. Biochemistry 2022, 61 (14) , 1465-1472. https://doi.org/10.1021/acs.biochem.2c00184
    10. Qiuchen Zheng, Bethany Lee, Micheal T. Kebede, Valerie A. Ivancic, Merc M. Kemeh, Henrique Lemos Brito, Donald E. Spratt, Noel D. Lazo. Exchange Broadening Underlies the Enhancement of IDE-Dependent Degradation of Insulin by Anionic Membranes. ACS Omega 2022, 7 (28) , 24757-24765. https://doi.org/10.1021/acsomega.2c02747
    11. Nadav Benhamou Goldfajn, Huayuan Tang, Feng Ding. Substoichiometric Inhibition of Insulin against IAPP Aggregation Is Attenuated by the Incompletely Processed N-Terminus of proIAPP. ACS Chemical Neuroscience 2022, 13 (13) , 2006-2016. https://doi.org/10.1021/acschemneuro.2c00231
    12. Huayuan Tang, Yunxiang Sun, Feng Ding. Hydrophobic/Hydrophilic Ratio of Amphiphilic Helix Mimetics Determines the Effects on Islet Amyloid Polypeptide Aggregation. Journal of Chemical Information and Modeling 2022, 62 (7) , 1760-1770. https://doi.org/10.1021/acs.jcim.1c01566
    13. Yijing Dang, Yi Lai, Fengping Chen, Qian Sun, Chunyong Ding, Wen Zhang, Zhiai Xu. Activatable NIR-II Fluorescent Nanoprobe for Rapid Detection and Imaging of Methylglyoxal Facilitated by the Local Nonpolar Microenvironment. Analytical Chemistry 2022, 94 (2) , 1076-1084. https://doi.org/10.1021/acs.analchem.1c04076
    14. Raliat O. Abioye, Ogadimma D. Okagu, Chibuike C. Udenigwe. Inhibition of Islet Amyloid Polypeptide Fibrillation by Structurally Diverse Phenolic Compounds and Fibril Disaggregation Potential of Rutin and Quercetin. Journal of Agricultural and Food Chemistry 2022, 70 (1) , 392-402. https://doi.org/10.1021/acs.jafc.1c06918
    15. Shani Ben-Zichri, Ravit Malishev, Ofek Oren, Daniel N. Bloch, Ran Taube, Niv Papo, Raz Jelinek. Bcl-2-Homology-Only Proapoptotic Peptides Modulate β-Amyloid Aggregation and Toxicity. ACS Chemical Neuroscience 2021, 12 (24) , 4554-4563. https://doi.org/10.1021/acschemneuro.1c00611
    16. Dieter Willbold, Birgit Strodel, Gunnar F. Schröder, Wolfgang Hoyer, Henrike Heise. Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids. Chemical Reviews 2021, 121 (13) , 8285-8307. https://doi.org/10.1021/acs.chemrev.1c00196
    17. GuangZhi Li, Dongmei Zhang. Research progress on the correlation between islet amyloid peptides and type 2 diabetes mellitus. Open Medicine 2025, 20 (1) https://doi.org/10.1515/med-2024-1124
    18. Li Wang, Sanghwan Park, Jae Hong Choi, Chang Young Lee, Kilho Eom, Taeyun Kwon. Molecular insight into cross-interaction between amyloid β isoforms and its effect on aggregation pathways. Journal of Biomolecular Structure and Dynamics 2025, , 1-11. https://doi.org/10.1080/07391102.2025.2475221
    19. Mansour A. Alsaleem, Hayder M. Al‐Kuraishy, Ali I. Al‐Gareeb, Maha M. Abdel‐Fattah, Mohammed Alrouji, Nasser A. Al‐Harchan, Mubarak Alruwaili, Marios Papadakis, Athanasios Alexiou, Gaber El‐Saber Batiha. Decrypting the Possible Mechanistic Role of Fenofibrate in Alzheimer's Disease and Type 2 Diabetes: The Truth and Mystery. Journal of Cellular and Molecular Medicine 2025, 29 (5) https://doi.org/10.1111/jcmm.70378
    20. Daniel Moreira-Silva, Melike Yuksel, Moorthi Ponnusamy, Mitchell T. Hansen, Joseph D. McMillan, Sneha Geethakrishnan, Shuai Wang, Lisa A. Collier, Gopal Thinakaran. Amylin exacerbates tau pathology in the visual cortex of diabetic mice by impairing lysosomal activity. Genes & Diseases 2025, 157 , 101602. https://doi.org/10.1016/j.gendis.2025.101602
    21. Huayuan Tang. Unveiling the inhibition mechanism of host-defense peptide cathelicidin LL-37 on the amyloid aggregation of the human islet amyloid polypeptide. Nanoscale 2025, 17 (9) , 5116-5127. https://doi.org/10.1039/D4NR05075D
    22. Sheng-Nan Wang, Xin-Yu Li, Zhong-Xia Lu, Lu-Xin Liu, Xuan-Ping Xu, Wen-Gong Yu, Xin-Zhi Lu. Effect and mechanism of oritavancin on hIAPP amyloid formation. Journal of Materials Chemistry B 2025, 13 (6) , 2192-2202. https://doi.org/10.1039/D4TB02215G
    23. Linwei Yang, Jingwei Zhang, James S. Andon, Lingjun Li, Tina Wang. Rapid discovery of cyclic peptide protein aggregation inhibitors by continuous selection. Nature Chemical Biology 2025, 86 https://doi.org/10.1038/s41589-024-01823-x
    24. Riyam N. Khalaf, Amal I. Hassan, Zeinab A. El-Shafiey, Abeer A. Faheim, Sattar S. Ibrahim, Hosam M. Saleh. Evaluation of an isatin-derived ligand and its metal complexes as potential anticancer agents in breast adenocarcinoma cells. Chemical Papers 2025, 1186 https://doi.org/10.1007/s11696-024-03873-w
    25. Cuiyun Gao, Zhiruo Wan, Yan Liu, Yuting Meng, Xu Chen, Xiaohan Tang, Lingyu Hang, Hailong Yuan. Flavones in pomelo peel resist fibril formation of human islet amyloid polypeptide. Chinese Herbal Medicines 2025, 17 (1) , 166-177. https://doi.org/10.1016/j.chmed.2024.02.002
    26. Jadon Sitton, Davis Pickett, Axell Rodriguez, Dmitry Kurouski. Lipids determine the toxicity of human islet polypeptide aggregates in vivo. Journal of Biological Chemistry 2025, 301 (1) , 108029. https://doi.org/10.1016/j.jbc.2024.108029
    27. Zhilong Wang, Jingjing Wei, Xuan Zhang, Haoran Ji, Shitao Fu, Zhonghong Gao, Hailing Li. Nitration of Tyr37 alters the aggregation pathway of hIAPP and enhances its cytotoxicity. International Journal of Biological Macromolecules 2025, 286 , 138367. https://doi.org/10.1016/j.ijbiomac.2024.138367
    28. Wenwen Yang, Jiayan Li, Jiayin Tian, Xiaoyi Liu, Wentao Xie, Xue Wu, Zhe Zhang, Yuefei Song, Shuya Wang, Shiyan Zhao, Zheng Wang, Yang Yang, Zhenxiao Jin. Pharmacological activity, phytochemistry, and organ protection of lithospermic acid. Journal of Cellular Physiology 2025, 240 (1) https://doi.org/10.1002/jcp.31460
    29. Raliat O. Abioye, Martha S. Yiridoe, Chenyang Wang, Tyler J. Avis, Tamer A. E. Ahmed, Riadh Hammami, Chibuike C. Udenigwe. Cross-domain binding of anti-fibrillation peptide TNGQ to islet amyloid polypeptide provides cytoprotective effects in giant unilamellar vesicles and pancreatic β-cells. Food & Function 2024, 15 (24) , 12047-12057. https://doi.org/10.1039/D4FO03322A
    30. Azadeh Hekmat, Irena Kostova, Ali Akbar Saboury. Application of metallic nanoparticles-amyloid protein supramolecular materials in tissue engineering and drug delivery: Recent progress and perspectives. Colloids and Surfaces B: Biointerfaces 2024, 244 , 114185. https://doi.org/10.1016/j.colsurfb.2024.114185
    31. Samuel D. McCalpin, Lucie Khemtemourian, Saba Suladze, Magdalena I. Ivanova, Bernd Reif, Ayyalusamy Ramamoorthy. Zinc and pH modulate the ability of insulin to inhibit aggregation of islet amyloid polypeptide. Communications Biology 2024, 7 (1) https://doi.org/10.1038/s42003-024-06388-y
    32. Jin Young Lim, Seo Yeon Kim, Ho-Tae Kim. Analysis of dimer and trimer complexes of the non-amyloidogenic rat islet amyloid polypeptide 21–37 by electrospray ionization-tandem mass spectrometry. European Journal of Mass Spectrometry 2024, 30 (5-6) , 254-260. https://doi.org/10.1177/14690667241278462
    33. Chin-Yu Lin, Cheng-Hong Hsieh, Pei-Yu Lai, Ching-Wei Huang, Yung-Hui Chung, Shang-Ming Huang, Kuo-Chiang Hsu. Inhibitory Effects of Gliadin Hydrolysates on BACE1 Expression and APP Processing to Prevent Aβ Aggregation. International Journal of Molecular Sciences 2024, 25 (23) , 13212. https://doi.org/10.3390/ijms252313212
    34. Hui Wang, Lin-Lin Xu, Lin-Qi Shi, Ru-Jiang Ma. Nanochaperones Based on Hydrophobic Interaction and Coordination Inhibit Protein Misfolding and Fibrillation. Chinese Journal of Polymer Science 2024, 42 (11) , 1710-1718. https://doi.org/10.1007/s10118-024-3169-6
    35. Arya R. Naik, Shreyada N. Save, Soumya S. Sahoo, Saurabh S. Yadav, Ashutosh Kumar, Jeetender Chugh, Shilpy Sharma. Metabolic perturbations associated with hIAPP-induced insulin resistance in skeletal muscles: Implications to the development of type 2 diabetes. The International Journal of Biochemistry & Cell Biology 2024, 176 , 106665. https://doi.org/10.1016/j.biocel.2024.106665
    36. Zhiyuan Song, Huayuan Tang, Adam Gatch, Yunxiang Sun, Feng Ding. Islet amyloid polypeptide fibril catalyzes amyloid-β aggregation by promoting fibril nucleation rather than direct axial growth. International Journal of Biological Macromolecules 2024, 279 , 135137. https://doi.org/10.1016/j.ijbiomac.2024.135137
    37. Anisha Manchanda, Bhupesh Goyal. Deciphering the impact of F23L mutation on the aggregation propensity of human islet amyloid polypeptide using molecular simulations. Journal of Molecular Liquids 2024, 411 , 125775. https://doi.org/10.1016/j.molliq.2024.125775
    38. Alexa Kamboukos, Billy J. Williams-Noonan, Patrick Charchar, Irene Yarovsky, Nevena Todorova. Graphitic nanoflakes modulate the structure and binding of human amylin. Nanoscale 2024, 16 (36) , 16870-16886. https://doi.org/10.1039/D4NR01315H
    39. Sindhujit Roy, Venkat Ramanan Srinivasan, Subash Arunagiri, Nishant Mishra, Anubhuti Bhatia, Kiran P. Shejale, Kailash Prasad Prajapati, Karunakar Kar, Bibin Gnanadhason Anand. Molecular insights into the phase transition of lysozyme into amyloid nanostructures: Implications of therapeutic strategies in diverse pathological conditions. Advances in Colloid and Interface Science 2024, 331 , 103205. https://doi.org/10.1016/j.cis.2024.103205
    40. Samuel D. McCalpin, Lina Mechakra, Magdalena I. Ivanova, Ayyalusamy Ramamoorthy. Differential effects of ganglioside lipids on the conformation and aggregation of islet amyloid polypeptide. Protein Science 2024, 33 (8) https://doi.org/10.1002/pro.5119
    41. Md. Niaj Morshed, Muhammad Awais, Reshmi Akter, Juha Park, Li Ling, Byoung Man Kong, Deok Chun Yang, Dong Uk Yang, Se Chan Kang, Seok-Kyu Jung. Exploring the therapeutic potential of Terminalia ferdinandiana (Kakadu Plum) in targeting obesity-induced Type 2 diabetes and chronic inflammation: An in silico and experimental study. South African Journal of Botany 2024, 171 , 32-44. https://doi.org/10.1016/j.sajb.2024.05.056
    42. Bryan A. Bogin, Zachary A. Levine. Drugging Disordered Proteins by Conformational Selection to Inform Therapeutic Intervention. 2024https://doi.org/10.1101/2024.07.03.601611
    43. Basiru Olaitan Ajiboye, Courage Dele Famusiwa, Monsurah Oluwaseyifunmi Amuda, Stephen Oluwaseun Afolabi, Benjamin Temidayo Ayotunde, Adedeji A. Adejumo, Ajoke Fehintola Idayat Akindele, Babatunji Emmanuel Oyinloye, Olutunmise Victoria Owolabi, Claudia Genovese, Oluwafemi Adeleke Ojo. Attenuation of PI3K/AKT signaling pathway by Ocimum gratissimum leaf flavonoid-rich extracts in streptozotocin-induced diabetic male rats. Biochemistry and Biophysics Reports 2024, 38 , 101735. https://doi.org/10.1016/j.bbrep.2024.101735
    44. Yuji Goto, Kichitaro Nakajima, Suguru Yamamoto, Keiichi Yamaguchi. Supersaturation, a Critical Factor Underlying Proteostasis of Amyloid Fibril Formation. Journal of Molecular Biology 2024, 436 (14) , 168475. https://doi.org/10.1016/j.jmb.2024.168475
    45. Samuel D. McCalpin, Lina Mechakra, Magdalena I. Ivanova, Ayyalusamy Ramamoorthy. Differential Effects of Ganglioside Lipids on the Conformation and Aggregation of Islet Amyloid Polypeptide. 2024https://doi.org/10.1101/2024.05.26.595964
    46. José Laxio Arenas, Jacopo Lesma, Tap Ha‐Duong, Bikash Ranjan Sahoo, Ayyalusamy Ramamoorthy, Nicolo Tonali, Jean‐Louis Soulier, Frédéric Halgand, François Giraud, Benoît Crousse, Julia Kaffy, Sandrine Ongeri. Composition and Conformation of Hetero‐ versus Homo‐Fluorinated Triazolamers Influence their Activity on Islet Amyloid Polypeptide Aggregation. Chemistry – A European Journal 2024, 30 (28) https://doi.org/10.1002/chem.202303887
    47. Tanishka Mehta, Bhupesh Goyal. Delineating the impact of N21D mutation on the conformational preferences and structural transitions in human islet amyloid polypeptide. Journal of Molecular Liquids 2024, 401 , 124528. https://doi.org/10.1016/j.molliq.2024.124528
    48. Mehmet Akdag, Vera van Schijndel, Tessa Sinnige. Islet amyloid polypeptide tagged with green fluorescent protein localises to mitochondria and forms filamentous aggregates in Caenorhabditis elegans. Biophysical Chemistry 2024, 307 , 107180. https://doi.org/10.1016/j.bpc.2024.107180
    49. Abid Ali, Tianyi Dou, Aidan P. Holman, Andrew Hung, Luke Osborne, Davis Pickett, Axell Rodriguez, Kiryl Zhaliazka, Dmitry Kurouski. The influence of zwitterionic and anionic phospholipids on protein aggregation. Biophysical Chemistry 2024, 306 , 107174. https://doi.org/10.1016/j.bpc.2024.107174
    50. Surajit Bhattacharjya, Zhizhuo Zhang, Ayyalusamy Ramamoorthy. LL-37: Structures, Antimicrobial Activity, and Influence on Amyloid-Related Diseases. Biomolecules 2024, 14 (3) , 320. https://doi.org/10.3390/biom14030320
    51. Qin Qiao, Guanghong Wei, Zhijian Song. Structural diversity in the membrane-bound hIAPP dimer correlated with distinct membrane disruption mechanisms. Physical Chemistry Chemical Physics 2024, 26 (8) , 7090-7102. https://doi.org/10.1039/D3CP05887E
    52. Lauryn Grcic, Grace Leech, Kalvin Kwan, Tim Storr. Targeting misfolding and aggregation of the amyloid-β peptide and mutant p53 protein using multifunctional molecules. Chemical Communications 2024, 60 (11) , 1372-1388. https://doi.org/10.1039/D3CC05834D
    53. Natalia Santos, Luthary Segura, Amber Lewis, Thuong Pham, Kwan H. Cheng. Multiscale Modeling of Macromolecular Interactions between Tau-Amylin Oligomers and Asymmetric Lipid Nanodomains That Link Alzheimer’s and Diabetic Diseases. Molecules 2024, 29 (3) , 740. https://doi.org/10.3390/molecules29030740
    54. Sofia Serravalle, Martina Pisano, Michele F. M. Sciacca, Nancy Salamone, Luciano Sicali, Giuseppe Mazzara, Luca Costa, Carmelo La Rosa. Critical micellar concentration determination of pure phospholipids and lipid‐raft and their mixtures with cholesterol. Proteins: Structure, Function, and Bioinformatics 2024, 47 https://doi.org/10.1002/prot.26669
    55. Seifollah Bahramikia, Nasrin Shirzadi, Nasim Pirmohammadi. Investigation of the Effect of Pyrogallol on the Formation of Amylin Amyloid Fibrils as a Strategy for the Treatment of Type 2 Diabetic Patients: A Theoretical and Experimental Study. Journal of Fluorescence 2024, 34 (1) , 245-251. https://doi.org/10.1007/s10895-023-03259-3
    56. Kendall B. E. Moore, Natalie G. Horgan, Brooke Lenters, Jessica S. Fortin. Diabetes mellitus drug discovery: insights into targeting feline and human amylin with small molecules. Veterinary Quarterly 2023, 43 (1) , 1-12. https://doi.org/10.1080/01652176.2023.2260442
    57. Per Hammarström, Sofie Nyström. Viruses and amyloids - a vicious liaison. Prion 2023, 17 (1) , 82-104. https://doi.org/10.1080/19336896.2023.2194212
    58. John Tower. Markers and mechanisms of death in Drosophila. Frontiers in Aging 2023, 4 https://doi.org/10.3389/fragi.2023.1292040
    59. Rongrong Wu, Zengkai Wang, Zili Jia, Chenglong Li, Jie Wang, Lei Liu, Mingdong Dong. Identification of hybrid amyloid strains assembled from amyloid-β and human islet amyloid polypeptide. Nanotechnology 2023, 34 (50) , 505101. https://doi.org/10.1088/1361-6528/acf3ee
    60. Boqi Yang, Tong Lu, Shuyu Wang, Chengyao Li, Chen Li, Fei Li. Interfacial effect on the ability of peptide-modified gold nanoclusters to inhibit hIAPP fibrillation and cytotoxicity. Biochimica et Biophysica Acta (BBA) - Biomembranes 2023, 1865 (8) , 184202. https://doi.org/10.1016/j.bbamem.2023.184202
    61. Zhen Zhang, Mengqiu Zhong, Haosheng Xiang, Yugao Ding, Yilong Wang, Yijing Shi, Guang Yang, Biao Tang, Kam C. Tam, Guofu Zhou. Antibacterial polylactic acid fabricated via Pickering emulsion approach with polyethyleneimine and polydopamine modified cellulose nanocrystals as emulsion stabilizers. International Journal of Biological Macromolecules 2023, 253 , 127263. https://doi.org/10.1016/j.ijbiomac.2023.127263
    62. Wenhao Fu, Huanyu Chi, Xin Dai, Hongni Zhu, Vince St. Dollente Mesias, Wei Liu, Jinqing Huang. Efficient optical plasmonic tweezer-controlled single-molecule SERS characterization of pH-dependent amylin species in aqueous milieus. Nature Communications 2023, 14 (1) https://doi.org/10.1038/s41467-023-42812-3
    63. Ayako Fukunaka, Mari Shimura, Takayuki Ichinose, Ofejiro B. Pereye, Yuko Nakagawa, Yasuko Tamura, Wakana Mizutani, Ryota Inoue, Takato Inoue, Yuto Tanaka, Takashi Sato, Tatsuya Saitoh, Toshiyuki Fukada, Yuya Nishida, Takeshi Miyatsuka, Jun Shirakawa, Hirotaka Watada, Satoshi Matsuyama, Yoshio Fujitani. Zinc and iron dynamics in human islet amyloid polypeptide-induced diabetes mouse model. Scientific Reports 2023, 13 (1) https://doi.org/10.1038/s41598-023-30498-y
    64. Jakub W. Wojciechowski, Witold Szczurek, Natalia Szulc, Monika Szefczyk, Malgorzata Kotulska. PACT - Prediction of amyloid cross-interaction by threading. Scientific Reports 2023, 13 (1) https://doi.org/10.1038/s41598-023-48886-9
    65. Mohammed Alrouji, Hayder M. Al-Kuraishy, Ali I. Al-Gareeb, Athanasios Alexiou, Marios Papadakis, Hebatallah M. Saad, Gaber El-Saber Batiha. The potential role of human islet amyloid polypeptide in type 2 diabetes mellitus and Alzheimer’s diseases. Diabetology & Metabolic Syndrome 2023, 15 (1) https://doi.org/10.1186/s13098-023-01082-1
    66. Natalia Santos, Luthary Segura, Amber Lewis, Thuong Pham, Kwan H. Cheng. Molecular Mechanisms of Protein–Lipid Interactions and Protein Folding of Heterogeneous Amylin and Tau Oligomers on Lipid Nanodomains That Link to Alzheimer’s. Macromol 2023, 3 (4) , 805-827. https://doi.org/10.3390/macromol3040046
    67. Yijing Tang, Dong Zhang, Xiong Gong, Jie Zheng. Multi-target amyloid probing and inhibition using basic orange fluorescence. Sensors & Diagnostics 2023, 2 (6) , 1469-1482. https://doi.org/10.1039/D3SD00124E
    68. Pengxiang Zhao, Zichen Zhao, Ziwei Yu, Lupeng Chen, Yi Jin, Jian Wu, Zhuqing Ren. Application of synthetic lipid droplets in metabolic diseases. Clinical and Translational Medicine 2023, 13 (11) https://doi.org/10.1002/ctm2.1441
    69. Danni Li, Yeyang Ma, Wencheng Xia, Youqi Tao, Yiling Zhang, Hong Zhang, Dan Li, Bin Dai, Cong Liu. Creating an Amyloid ‘Kaleidoscope’ Using Short Iodinated Peptides. Angewandte Chemie 2023, 135 (42) https://doi.org/10.1002/ange.202310737
    70. Danni Li, Yeyang Ma, Wencheng Xia, Youqi Tao, Yiling Zhang, Hong Zhang, Dan Li, Bin Dai, Cong Liu. Creating an Amyloid ‘Kaleidoscope’ Using Short Iodinated Peptides. Angewandte Chemie International Edition 2023, 62 (42) https://doi.org/10.1002/anie.202310737
    71. Zhiying Li, Jinlong Tian, Zhen Cheng, Wei Teng, Weijia Zhang, Yiwen Bao, Yidi Wang, Baoge Song, Yi Chen, Bin Li. Hypoglycemic bioactivity of anthocyanins: A review on proposed targets and potential signaling pathways. Critical Reviews in Food Science and Nutrition 2023, 63 (26) , 7878-7895. https://doi.org/10.1080/10408398.2022.2055526
    72. Uma Sankar Mondal, Subhankar Paul. Inhibition of hen egg white lysozyme fibrillation by a self-assembled nanostructured lysozyme and graphene oxide conjugate. New Journal of Chemistry 2023, 47 (38) , 17666-17678. https://doi.org/10.1039/D3NJ02831C
    73. Deepika Regmi, Fengyun Shen, Aleksander Stanic, Majedul Islam, Deguo Du. Effect of phospholipid liposomes on prion fragment (106–128) amyloid formation. Biochimica et Biophysica Acta (BBA) - Biomembranes 2023, 1865 (7) , 184199. https://doi.org/10.1016/j.bbamem.2023.184199
    74. Ramona Clemen, Eduardo Fuentes-Lemus, Sander Bekeschus, Michael J. Davies. Oxidant-modified amylin fibrils and aggregates alter the inflammatory profile of multiple myeloid cell types, but are non-toxic to islet β cells. Redox Biology 2023, 65 , 102835. https://doi.org/10.1016/j.redox.2023.102835
    75. Yijing Tang, Dong Zhang, Xiong Gong, Jie Zheng. Cross-seeding enables repurposing of aurein antimicrobial peptides as a promoter of human islet amyloid polypeptide (hIAPP). Journal of Materials Chemistry B 2023, 11 (33) , 7920-7932. https://doi.org/10.1039/D3TB01099F
    76. Ming-Hao Li, Xiaoxue Zhang, Erwin London, Daniel P. Raleigh. Impact of Ca2+ on membrane catalyzed IAPP amyloid formation and IAPP induced vesicle leakage. Biochimica et Biophysica Acta (BBA) - Biomembranes 2023, 1865 (6) , 184161. https://doi.org/10.1016/j.bbamem.2023.184161
    77. Avisek Bera, Pooja Ghosh, Shilpendu Ghosh, Arindam Mukherjee, Priyadarsi De. Antioxidant Polymers with Enhanced Neuroprotection Against Insulin Fibrillation. Macromolecular Bioscience 2023, 23 (7) https://doi.org/10.1002/mabi.202300100
    78. Unmesh D. Chowdhury, Arnav Paul, B.L. Bhargava. Interaction of the tau fibrils with the neuronal membrane. Biophysical Chemistry 2023, 298 , 107024. https://doi.org/10.1016/j.bpc.2023.107024
    79. Akira Naito, Izuru Kawamura. Dynamic membrane interaction and amyloid fibril formation of glucagon, melittin and human calcitonin. Biophysical Chemistry 2023, 298 , 107025. https://doi.org/10.1016/j.bpc.2023.107025
    80. Ali Abdulmawjood Mohammed, Sagar S. Barale, Subodh Ashok Kamble, Sneha B. Paymal, Kailas D. Sonawane. Molecular insights into the inhibition of early stages of Aβ peptide aggregation and destabilization of Alzheimer's Aβ protofibril by dipeptide D-Trp-Aib: A molecular modelling approach. International Journal of Biological Macromolecules 2023, 242 , 124880. https://doi.org/10.1016/j.ijbiomac.2023.124880
    81. Mohammed Alrouji, Hayder M. Al‐kuraishy, Ali I. Al‐Gareeb, Athanasios Alexiou, Marios Papadakis, Majid S. Jabir, Hebatallah M. Saad, Gaber El‐Saber Batiha. NF‐κB/NLRP3 inflammasome axis and risk of Parkinson's disease in Type 2 diabetes mellitus: A narrative review and new perspective. Journal of Cellular and Molecular Medicine 2023, 27 (13) , 1775-1789. https://doi.org/10.1111/jcmm.17784
    82. Haruka Kawabe, Satoshi Ikawa, Katsuhisa Kitano, Tamotsu Zako. Peroxynitric acid inhibits amyloid β aggregation. Biochemical and Biophysical Research Communications 2023, 660 , 1-5. https://doi.org/10.1016/j.bbrc.2023.03.060
    83. Xing-Yu Liu, Shuai-Chen Du, Shu-Lan Li, Feng-Lei Jiang, Peng Jiang, Yi Liu. Inhibition mechanism of human insulin fibrillation by Bodipy carbon polymer dots and photothermal defibrillation effect of Bodipy carbon polymer dots modified by ThT. Biophysical Chemistry 2023, 297 , 107009. https://doi.org/10.1016/j.bpc.2023.107009
    84. Debabrata Maity. Recent advances in the modulation of amyloid protein aggregation using the supramolecular host-guest approaches. Biophysical Chemistry 2023, 297 , 107022. https://doi.org/10.1016/j.bpc.2023.107022
    85. Dipanwita Roy, Narayan Chandra Maity, Sourav Kumar, Anupam Maity, Bhisma N. Ratha, Ranjit Biswas, Nakul Chandra Maiti, Atin Kumar Mandal, Anirban Bhunia. Modulatory role of copper on hIAPP aggregation and toxicity in presence of insulin. International Journal of Biological Macromolecules 2023, 241 , 124470. https://doi.org/10.1016/j.ijbiomac.2023.124470
    86. Kai Wang, Kun Yao, Xu-Yang Chen, Da-Ke Wen, Ya-Juan Qin, Zhi-Gang Hu, Yu-Shun Yang. Discovery of the cysteine dynamics during the development and treatment of diabetic process by fluorescent imaging. Redox Biology 2023, 62 , 102660. https://doi.org/10.1016/j.redox.2023.102660
    87. Liyuan Zhao, Liang Luo, Fanling Meng. Metal-mediated nanobody assemblies as potent alleviators of human islet amyloid polypeptide aggregation. Materials Chemistry Frontiers 2023, 7 (10) , 2068-2077. https://doi.org/10.1039/D2QM01372J
    88. Amber Lewis, Thuong Pham, Ngoc Nguyen, Angela Graf, Kwan H. Cheng. Lipid domain boundary triggers membrane damage and protein folding of human islet amyloid polypeptide in the early pathogenesis of amyloid diseases. Biophysical Chemistry 2023, 296 , 106993. https://doi.org/10.1016/j.bpc.2023.106993
    89. Faisal Holil AlAnazi, Hayder M. Al‐kuraishy, Ali I. Al‐Gareeb, Athanasios Alexiou, Marios Papadakis, Hanan A. Ogaly, Yousef Abud Alanazi, Hebatallah M. Saad, Gaber El‐Saber Batiha. Effects of neprilysin and neprilysin inhibitors on glucose homeostasis: Controversial points and a promising arena. Journal of Diabetes 2023, 15 (5) , 397-408. https://doi.org/10.1111/1753-0407.13389
    90. Emile de Bruyn, Anton Emil Dorn, Olav Zimmermann, Giulia Rossetti. SPEADI: Accelerated Analysis of IDP-Ion Interactions from MD-Trajectories. Biology 2023, 12 (4) , 581. https://doi.org/10.3390/biology12040581
    91. Mathew Sebastiao, Margaryta Babych, Noé Quittot, Kiran Kumar, Alexandre A. Arnold, Isabelle Marcotte, Steve Bourgault. Development of a novel fluorescence assay for studying lipid bilayer perturbation induced by amyloidogenic peptides using cell plasma membrane vesicles. Biochimica et Biophysica Acta (BBA) - Biomembranes 2023, 1865 (3) , 184118. https://doi.org/10.1016/j.bbamem.2022.184118
    92. Aranyak Mitra, Amit Mitra, Nandini Sarkar. Differential effects of DTT on HEWL amyloid fibrillation and fibril morphology at different pH. Biophysical Chemistry 2023, 294 , 106962. https://doi.org/10.1016/j.bpc.2023.106962
    93. Jong-Min Suh, Mingeun Kim, Jeasang Yoo, Jiyeon Han, Cinthya Paulina, Mi Hee Lim. Intercommunication between metal ions and amyloidogenic peptides or proteins in protein misfolding disorders. Coordination Chemistry Reviews 2023, 478 , 214978. https://doi.org/10.1016/j.ccr.2022.214978
    94. Songfeng Yu, Wenjun Wang, Shanshan Li, Jiaheng Li, Runan Zhao, Donghong Liu, Jianping Wu. Glucoregulatory Properties of Fermented Soybean Products. Fermentation 2023, 9 (3) , 254. https://doi.org/10.3390/fermentation9030254
    95. Carola Rando, Giuseppe Grasso, Dibakar Sarkar, Michele Francesco Maria Sciacca, Lorena Maria Cucci, Alessia Cosentino, Giuseppe Forte, Martina Pannuzzo, Cristina Satriano, Anirban Bhunia, Carmelo La Rosa. GxxxG Motif Stabilize Ion-Channel like Pores through Cα―H···O Interaction in Aβ (1-40). International Journal of Molecular Sciences 2023, 24 (3) , 2192. https://doi.org/10.3390/ijms24032192
    96. Debabrata Maity. Inhibition of Amyloid Protein Aggregation Using Selected Peptidomimetics. ChemMedChem 2023, 18 (2) https://doi.org/10.1002/cmdc.202200499
    97. Elena Quigley, Bradley L. Nilsson. β-Sheet and β-Hairpin Peptide Nanomaterials. 2023, 53-86. https://doi.org/10.1007/978-3-031-29360-3_2
    98. Barend O.W. Elenbaas, Stefanie M. Kremsreiter, Lucie Khemtemourian, J. Antoinette Killian, Tessa Sinnige. Fibril elongation by human islet amyloid polypeptide is the main event linking aggregation to membrane damage. BBA Advances 2023, 3 , 100083. https://doi.org/10.1016/j.bbadva.2023.100083
    99. Rolf Antonie Loch, Hongzhi Wang, Alex Perálvarez-Marín, Philipp Berger, Henrietta Nielsen, Angeliki Chroni, Jinghui Luo. Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseases. Computational and Structural Biotechnology Journal 2023, 21 , 1189-1204. https://doi.org/10.1016/j.csbj.2023.01.022
    100. Qing-Rong Liu, Min Zhu, Qinghua Chen, Maja Mustapic, Dimitrios Kapogiannis, Josephine M. Egan. Novel Hominid-Specific IAPP Isoforms: Potential Biomarkers of Early Alzheimer’s Disease and Inhibitors of Amyloid Formation. Biomolecules 2023, 13 (1) , 167. https://doi.org/10.3390/biom13010167
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    Cite this: Chem. Rev. 2021, 121, 3, 1845–1893
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    Published January 11, 2021
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