Impact of the S20G Mutation on the Structural and Aggregation Properties of hIAPP Monomers 


Vol. 69,  No. 4, pp. 177-183, Aug.  2025
10.5012/jkcs.2025.69.4.177


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  Abstract

Type 2 diabetes (T2D), the predominant form of diabetes (>90% of cases), is characterized by human islet amyloid polypeptide (hIAPP) amyloid deposits resulting from protein misfolding. The serine-to-glycine mutation at position 20 (S20G) in hIAPP is associated with T2D in certain populations, yet its molecular impact on conformation and aggregation remains poorly understood. This study employs replica-exchange molecular dynamics (REMD) simulations to investigate how the S20G mutation, combined with histidine behaviors (tautomerism and protonation), influences hIAPP monomer structural and aggregation properties. We analyzed clustering, secondary structure, hydrogen bonds, and contact maps across three histidine states: hIAPP(ε), hIAPP(δ), and hIAPP(p). Our findings reveal distinct conformational tendencies, providing novel insights into the mechanisms underlying hIAPP misfolding in T2D.

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  Cite this article

[IEEE Style]

C. Wang, P. Li, X. Pu, B. Kang, "Impact of the S20G Mutation on the Structural and Aggregation Properties of hIAPP Monomers," Journal of the Korean Chemical Society, vol. 69, no. 4, pp. 177-183, 2025. DOI: 10.5012/jkcs.2025.69.4.177.

[ACM Style]

Chuanbo Wang, Pengfei Li, Xin Pu, and Baotao Kang. 2025. Impact of the S20G Mutation on the Structural and Aggregation Properties of hIAPP Monomers. Journal of the Korean Chemical Society, 69, 4, (2025), 177-183. DOI: 10.5012/jkcs.2025.69.4.177.

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ISSN(Print) 1017-2548
ISSN(Online) 2234-8530