Ontology highlight
ABSTRACT:
SUBMITTER: Wang W
PROVIDER: S-EPMC7688565 | biostudies-literature | 2020 Nov
REPOSITORIES: biostudies-literature
Wang Wenhua W Hansmann Ulrich H E UHE
The journal of physical chemistry. B 20201116 47
In systemic amyloidosis, serum amyloid A (SAA) fibril deposits cause widespread damages to tissues and organs that eventually may lead to death. A therapeutically intervention therefore has either to dissolve these fibrils or inhibit their formation. However, only recently has the human SAA fibril structure been resolved at a resolution that is sufficient for development of drug candidates. Here, we use molecular dynamic simulations to probe the factors that modulate the stability of this fibril ...[more]