Rapid restructurization of conformationally-distinct alpha-synuclein amyloid fibrils at an elevated temperature

PeerJ

article

Mantas Ziaunys¹  Andrius Sakalauskas¹  Kamile Mikalauskaite¹  Vytautas Smirnovas¹ 

[1] Institute of Biotechnology, Life Sciences Center, Vilnius University

关键词: Amyloid;    Alpha-synuclein;    Protein aggregation;    Protein fibrils;    Fibril structure;   

DOI  :  10.7717/peerj.14137

学科分类：社会科学、人文和艺术（综合）

来源: Inra

【 摘 要 】

Protein aggregation in the form of amyloid fibrils is linked with the onset and progression of more than 30 amyloidoses, including multiple neurodegenerative disorders, such as Alzheimer’s or Parkinson’s disease. Despite countless studies and years of research, the process of such aggregate formation is still not fully understood. One peculiar aspect of amyloids is that they appear to be capable of undergoing structural rearrangements even after the fibrils have already formed. Such a phenomenon was reported to occur in the case of alpha-synuclein and amyloid beta aggregates after a long period of incubation. In this work, we examine whether incubation at an elevated temperature can induce the restructurization of four different conformation alpha-synuclein amyloid fibrils. We show that this structural alteration occurs in a relatively brief time period, when the aggregates are incubated at 60 °C. Additionally, it appears that during this process multiple conformationally-distinct alpha-synuclein fibrils all shift towards an identical secondary structure.

【 授权许可】

CC BY