Humanin variants aggregate to produce different fibril morphologies.

ABSTRACT: Humanin is an endogenous human peptide with cytoprotective effects, including inhibition of apoptosis via interaction with BCL-2 proteins such as BAX. The therapeutic benefits of HN have been well-documented, and administering humanin and related endogenous human peptides for treatment of disease, aging, and enhancement of athletic performance is becoming more widespread. However, very little is known about the actual molecular structure of humanin and how it interacts with its protein partners. Here we present the amyloid-like β-sheet fibrillization of HN along with characterization of its secondary structure properties via transmission electron microscopy and other biophysical techniques. We identified several important HN mutants and documented their effects on the fibrillization proces

SUBMITTER: Morris DL 

PROVIDER: S-EPMC12281593 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature