γ-AApeptides-based Small Molecule Ligands That Disaggregate Human Islet Amyloid Polypeptide.

ABSTRACT: The abnormal folding and aggregation of functional proteins into amyloid is a typical feature of many age-related diseases, including Type II diabetes. Growing evidence has revealed that the prevention of aggregate formation in culprit proteins could retard the progression of amyloid diseases. Human Amylin, also known as human islet amyloid polypeptide (hIAPP), is the major factor for categorizing Type II diabetes as an amyloid disease. Specifically, hIAPP has a great aggregation potential, which always results in a lethal situation for the pancreas. Many peptide inhibitors have been constructed from the various segments of the full-length hIAPP peptide; however, only a few have their origin from the screening of combinatorial peptidomimetic library. In this study, based on HW-155, which w

SUBMITTER: Bolarinwa O 

PROVIDER: S-EPMC6952368 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature