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ShanghaiTech University Knowledge Management System
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]) |
ISSN | 1530-6984 |
EISSN | 1530-6992 |
卷号 | 25期号:9页码:3653-3661 |
发表状态 | 已发表 |
DOI | 10.1021/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 |
URL | 查看原文 |
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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