Effect of TMAO and Urea on Dimers and Tetramers of Amyloidogenic Heptapeptides (²³FGAILSS²⁹).

ABSTRACT: Human islet amyloid polypeptide (hIAPP) (1-37) is an intrinsically disordered protein that is released with insulin by β-cells found in the pancreas. Under certain environmental conditions, hIAPP can aggregate, which leads to β-cell death. FGAILSS (23-29) residues of the hIAPP protein form β sheets, which may be toxic species in type 2 diabetes (T2D) patients. All-atom molecular dynamics (MD) simulations have been used to analyze the effect of two distinct types of osmolytes trimethylamine N-oxide (TMAO) and urea on two and four FGAILSS heptapeptides. TMAO leads the individual peptide toward an extended conformation with a higher radius of gyration and favors the formation of antiparallel β-sheets with an increase in its concentration. However, urea mostly shows compaction of individual pe

SUBMITTER: Khan A 

PROVIDER: S-EPMC7593999 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature