Abstract:
:Several pathological disorders have known linkages with the misfolding and abnormal oligomerization of peptides and proteins and their accumulation into numerous aggregates. One such peptide is human islet amyloid polypeptide (hIAPP) responsible for amyloid aggregation in type 2 diabetes. This aggregation can be altered by osmolytes, which are natural agents that can alter the environment surrounding of hIAPP. Here, we implemented several replica-exchange molecular dynamics (REMD) simulations to examine the effects of the denaturing osmolyte urea and the protective osmolyte trimethylamine N-oxide (TMAO) on amyloid aggregation and on the conformational ensemble of the hIAPP peptide. We analyzed specific modulations in hIAPP peptide and observed a state shift in the conformational population of hIAPP. Our results confirmed that urea restricted the peptide aggregation and led to the formation of unfolded conformations, whereas TMAO promoted folding and a compact state of the hIAPP peptide.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Kumari A,Sharma R,Somvanshi P,Grover Adoi
10.1016/j.ijbiomac.2020.08.104subject
Has Abstractpub_date
2020-12-01 00:00:00pages
2569-2582eissn
0141-8130issn
1879-0003pii
S0141-8130(20)34192-1journal_volume
164pub_type
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