Deciphering the influence of Y12L and N17H substitutions on the conformation and oligomerization of human calcitonin-Reference-Cited by-同舟云学术

Deciphering the influence of Y12L and N17H substitutions on the conformation and oligomerization of human calcitonin

Published:2024 Issue:3 Volume:20 Page:693-703
ISSN:1744-683X
Container-title:Soft Matter
language:en
Short-container-title:Soft Matter

Author:

Yan Jiajia¹²,Wang Ying¹,Fan Xinjie¹,Zou Yu³^ORCID,Ding Feng⁴^ORCID,Huang Fengjuan²,Sun Yunxiang¹⁴^ORCID

Affiliation:

1. School of Physical Science and Technology, Ningbo University, Ningbo 315211, China

2. Ningbo Institute of Innovation for Combined Medicine and Engineering (NIIME), Ningbo Medical Center Lihuili Hospital, Ningbo 315211, China

3. Department of Sport and Exercise Science, Zhejiang University, Hangzhou 310058, China

4. Department of Physics and Astronomy, Clemson University, Clemson, SC 29634, USA

Abstract

Monomers of hCT primarily adopted dynamic helical structures and readily aggregated into β-sheet-rich oligomers and β-barrel intermediates. The Y12L and N17H mutations enhanced helical conformations and partially inhibited the helix-to-β conversion.

Funder

National Institutes of Health

National Natural Science Foundation of China

Natural Science Foundation of Ningbo Municipality

Publisher

Royal Society of Chemistry (RSC)

Subject

Condensed Matter Physics,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2024/SM/D3SM01332D

Reference55 articles.

1. Structural Biology of Calcitonin: From Aqueous Therapeutic Properties to Amyloid Aggregation

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