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

ABSTRACT: 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 cap

SUBMITTER: Mou HZ 

PROVIDER: S-EPMC10357426 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature