Molecular Interpretation of ACTH-β-endorphin Coaggregation: Relevance to Secretory Granule Biogenesis

Overview

Journal PLoS One

Specialties General Medicine
Science

Date 2012 Mar 10

PMID 22403619

Citations 5

Authors

Srivastav Ranganathan

Pradeep K Singh

Uday Singh

Praful S Singru

Ranjith Padinhateeri

Samir K Maji

Affiliations

Soon will be listed here.

Abstract

Peptide/protein hormones could be stored as non-toxic amyloid-like structures in pituitary secretory granules. ACTH and β-endorphin are two of the important peptide hormones that get co-stored in the pituitary secretory granules. Here, we study molecular interactions between ACTH and β-endorphin and their colocalization in the form of amyloid aggregates. Although ACTH is known to be a part of ACTH-β-endorphin aggregate, ACTH alone cannot aggregate into amyloid under various plausible conditions. Using all atom molecular dynamics simulation we investigate the early molecular interaction events in the ACTH-β-endorphin system, β-endorphin-only system and ACTH-only system. We find that β-endorphin and ACTH formed an interacting unit, whereas negligible interactions were observed between ACTH molecules in ACTH-only system. Our data suggest that ACTH is not only involved in interaction with β-endorphin but also enhances the stability of mixed oligomers of the entire system.

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