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Ambient Temperature Affects Protein Self-Assembly by Interfering with the Interfacial Aggregation Behavior

[Image: see text] Amyloid fibrillation is known to be associated with degenerative diseases, and mature fibrils are also considered as valuable biomedical materials. Thus, the mechanism and influencing factors of fibrillation have always been the focus of research. However, in vitro studies are alwa...

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Autores principales: Mou, Han-Zhang, Zhao, Cong-Lin, Song, Juan, Xing, Lei, Chen, Hong-Yuan, Xu, Jing-Juan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2023
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10357426/
https://www.ncbi.nlm.nih.gov/pubmed/37483188
http://dx.doi.org/10.1021/acsomega.3c01606
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author Mou, Han-Zhang
Zhao, Cong-Lin
Song, Juan
Xing, Lei
Chen, Hong-Yuan
Xu, Jing-Juan
author_facet Mou, Han-Zhang
Zhao, Cong-Lin
Song, Juan
Xing, Lei
Chen, Hong-Yuan
Xu, Jing-Juan
author_sort Mou, Han-Zhang
collection PubMed
description [Image: see text] Amyloid fibrillation is known to be associated with degenerative diseases, and mature fibrils are also considered as valuable biomedical materials. Thus, the mechanism and influencing factors of fibrillation have always been the focus of research. However, in vitro studies are always plagued by low reproducibility of kinetics and the molecular mechanism of amyloid fibrillation is under debate until now. Here, we identified the ambient temperature (AT) as a non-negligible interfering factor in in vitro self-assembly of globular protein hen egg-white lysozyme for the first time. By multimodal molecular spectroscopy methods, not only the effect of ATs on the kinetics of protein aggregation was described but also the conformational changes of the molecular structure with different ATs were captured. Through investigating the dependence of interfacial area and catalysis, the reason for this influence was construed by the various aggregation behaviors of protein molecules in the two-phase interface. The results suggest that in vitro mechanism research on protein fibrillation needs to first clarify the AT for a more accurate comparative analysis. The proposal of this concept will provide a new clue for a deeper understanding of the mechanism of protein self-assembly and may have an impact on evaluating the efficiency of amyloid accelerators or inhibitors based on the comparative analysis of protein self-assembly.
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spelling pubmed-103574262023-07-21 Ambient Temperature Affects Protein Self-Assembly by Interfering with the Interfacial Aggregation Behavior Mou, Han-Zhang Zhao, Cong-Lin Song, Juan Xing, Lei Chen, Hong-Yuan Xu, Jing-Juan ACS Omega [Image: see text] Amyloid fibrillation is known to be associated with degenerative diseases, and mature fibrils are also considered as valuable biomedical materials. Thus, the mechanism and influencing factors of fibrillation have always been the focus of research. However, in vitro studies are always plagued by low reproducibility of kinetics and the molecular mechanism of amyloid fibrillation is under debate until now. Here, we identified the ambient temperature (AT) as a non-negligible interfering factor in in vitro self-assembly of globular protein hen egg-white lysozyme for the first time. By multimodal molecular spectroscopy methods, not only the effect of ATs on the kinetics of protein aggregation was described but also the conformational changes of the molecular structure with different ATs were captured. Through investigating the dependence of interfacial area and catalysis, the reason for this influence was construed by the various aggregation behaviors of protein molecules in the two-phase interface. The results suggest that in vitro mechanism research on protein fibrillation needs to first clarify the AT for a more accurate comparative analysis. The proposal of this concept will provide a new clue for a deeper understanding of the mechanism of protein self-assembly and may have an impact on evaluating the efficiency of amyloid accelerators or inhibitors based on the comparative analysis of protein self-assembly. American Chemical Society 2023-07-07 /pmc/articles/PMC10357426/ /pubmed/37483188 http://dx.doi.org/10.1021/acsomega.3c01606 Text en © 2023 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Mou, Han-Zhang
Zhao, Cong-Lin
Song, Juan
Xing, Lei
Chen, Hong-Yuan
Xu, Jing-Juan
Ambient Temperature Affects Protein Self-Assembly by Interfering with the Interfacial Aggregation Behavior
title Ambient Temperature Affects Protein Self-Assembly by Interfering with the Interfacial Aggregation Behavior
title_full Ambient Temperature Affects Protein Self-Assembly by Interfering with the Interfacial Aggregation Behavior
title_fullStr Ambient Temperature Affects Protein Self-Assembly by Interfering with the Interfacial Aggregation Behavior
title_full_unstemmed Ambient Temperature Affects Protein Self-Assembly by Interfering with the Interfacial Aggregation Behavior
title_short Ambient Temperature Affects Protein Self-Assembly by Interfering with the Interfacial Aggregation Behavior
title_sort ambient temperature affects protein self-assembly by interfering with the interfacial aggregation behavior
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10357426/
https://www.ncbi.nlm.nih.gov/pubmed/37483188
http://dx.doi.org/10.1021/acsomega.3c01606
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