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β-Lactoglobulin forms a conserved fibril core that assembles into diverse fibril polymorphs
2025-02-24
发表期刊NANO LETTERS (IF:9.6[JCR-2023],10.1[5-Year])
ISSN1530-6984
EISSN1530-6992
卷号25期号:9页码:3653-3661
发表状态已发表
DOI10.1021/acs.nanolett.5c00137
摘要The beta-lactoglobulin (beta-LG) protein, sourced from dietary products, is notable for forming amyloid fibrils, which are increasingly recognized as valuable protein-based nanomaterials due to their superior cytocompatibility, chemical resilience, and mechanical characteristics. However, the precise atomic details of beta-LG's fibril assembly are not understood. In this study, we utilized cryo-electron microscopy to elucidate the composition and architecture of beta-LG fibrils. We discovered that the beta-LG fibril was rapidly assembled after a short time incubation. Remarkably, these fibril cores were composed of the first 32 residues, forming four beta-strands that adopted a serpentine arrangement into a single protofilament. This protofilament core's stability was reinforced by hydrophobic interactions. Two identical protofilaments then align to form four distinct structural polymorphs through unique interfacial configurations, which were stabilized by hydrophilic interactions, hydrogen bonding, and electrostatic forces. Our findings provide a structural framework for understanding beta-LG fibril formation and pave the way for designing innovative beta-LG-based nanomaterials.
关键词beta-lactoglobulin peptide self-assembly cryo-electron microscopy fibril polymorphs nanomaterials
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收录类别SCI ; EI
语种英语
资助项目National Natural Science Foundation (NSF) of China["22425704","82188101","32171236","92353302","32170683"] ; Science and Technology Commission of Shanghai Municipality (STCSM)[22JC1410400] ; Shanghai Pilot Program for Basic Research - Chinese Academy of Science, Shanghai Branch[JCYJ-SHFY-2022-005] ; CAS Project for Young Scientists in Basic Research[YSBR-095] ; Strategic Priority Research Program of the Chinese Academy of Sciences[XDB1060000]
WOS研究方向Chemistry ; Science & Technology - Other Topics ; Materials Science ; Physics
WOS类目Chemistry, Multidisciplinary ; Chemistry, Physical ; Nanoscience & Nanotechnology ; Materials Science, Multidisciplinary ; Physics, Applied ; Physics, Condensed Matter
WOS记录号WOS:001432989800001
出版者AMER CHEMICAL SOC
EI入藏号20250917960456
EI主题词Hydrogen bonds
EI分类号214 Materials Science - 801.3 Physical Chemistry
原始文献类型Article in Press
文献类型期刊论文
条目标识符https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/490287
专题生命科学与技术学院_PI研究组_孙博组
共同第一作者Li, Danni
通讯作者Dai, Bin
作者单位
1.School of Sensing Science and Engineering, School of Electronic Information and Electrical Engineering, Shanghai Jiao Tong University, Shanghai 200240, China
2.Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders (Ministry of Education), Shanghai Jiao Tong University, Shanghai, 200030, China
3.Zhangjiang Institute for Advanced Study, Shanghai Jiao Tong University, Shanghai 200240, China
4.School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China
5.Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 201210, China
6.State Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 200032, China
7.Shanghai Academy of Natural Sciences (SANS), Fudan University, Shanghai, China
推荐引用方式
GB/T 7714
Xu, Yongyi,Li, Danni,Zhang, Yiling,et al. β-Lactoglobulin forms a conserved fibril core that assembles into diverse fibril polymorphs[J]. NANO LETTERS,2025,25(9):3653-3661.
APA Xu, Yongyi.,Li, Danni.,Zhang, Yiling.,Zhao, Qiuyue.,Sun, Bo.,...&Dai, Bin.(2025).β-Lactoglobulin forms a conserved fibril core that assembles into diverse fibril polymorphs.NANO LETTERS,25(9),3653-3661.
MLA Xu, Yongyi,et al."β-Lactoglobulin forms a conserved fibril core that assembles into diverse fibril polymorphs".NANO LETTERS 25.9(2025):3653-3661.
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