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Molecular Interpretation of ACTH-b-Endorphin Coaggregation: Relevance to Secretory Granule Biogenesis.
- Source :
- PLoS ONE; Mar2012, Vol. 7 Issue 3, p1-12, 12p
- Publication Year :
- 2012
-
Abstract
- Peptide/protein hormones could be stored as non-toxic amyloid-like structures in pituitary secretory granules. ACTH and βendorphin 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. [ABSTRACT FROM AUTHOR]
- Subjects :
- PROTEIN hormones
PEPTIDES
AMYLOID
SECRETORY granules
MOLECULAR dynamics
ENDORPHINS
Subjects
Details
- Language :
- English
- ISSN :
- 19326203
- Volume :
- 7
- Issue :
- 3
- Database :
- Complementary Index
- Journal :
- PLoS ONE
- Publication Type :
- Academic Journal
- Accession number :
- 79930415
- Full Text :
- https://doi.org/10.1371/journal.pone.0031924