Paper Citing NAMD - Abstract
Ranganathan, Srivastav; Singh, Pradeep K.; Singh, Uday; Singru, Praful S.; Padinhateeri, Ranjith; Maji, Samir K.
Molecular Interpretation of ACTH-beta-Endorphin Coaggregation: Relevance to Secretory Granule Biogenesis
PLOS ONE, 7 Art. No. e31924, MAR 5 2012
Peptide/protein hormones could be stored as non-toxic amyloid-like structures in pituitary secretory granules. ACTH and beta-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 beta-endorphin and their colocalization in the form of amyloid aggregates. Although ACTH is known to be a part of ACTH-beta-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-beta-endorphin system, beta-endorphin-only system and ACTH-only system. We find that beta-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 beta-endorphin but also enhances the stability of mixed oligomers of the entire system.
