Amyloid Self-Assembly: From Fibrillation to Crystallization

Yin Wang

Publikation: Bog/antologi/afhandling/rapportPh.d.-afhandling

Abstract

Amyloid self-assembly is one important kind of protein aggregates due to protein misfolding. On one hand, amyloid aggregates are usually associated with human diseases; on the other hand, the amyloid self-assembly has been considered as the new bottom-up approaches to developing the protein toolkit for artificial functional biomaterials. Thus, the investigation in mechanism of amyloid self-organization is favorable to understanding of pathological mechanism underlying the amyloid plaques as well as molecular design of amyloid peptide for biomimetic materials. The conversion of soluble peptide monomers into insoluble amyloid aggregates is a hierarchical assembling process driven by different non-covalent interactions, producing a variety of kinetically trapped intermediates at transition states and thermodynamically favorable products with the minimal energy level. In this thesis, the hierarchical fibrillation of amyloid assembly, pH-induced reversible crystallization of amyloid peptide and DMSOswitched crystallization of α-helical amyloid peptide are explored to give an insight into the intrinsic mechanism for hierarchical self-assembly of amyloid fibrillation and external factors that induce the controllable phase transformation. It can be expected to utilize these strategies to controllably assemble the desired amyloid architectures
OriginalsprogEngelsk
ForlagÅrhus Universitet
Antal sider106
StatusUdgivet - jun. 2022

Fingeraftryk

Dyk ned i forskningsemnerne om 'Amyloid Self-Assembly: From Fibrillation to Crystallization'. Sammen danner de et unikt fingeraftryk.

Citationsformater