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Molecular Interpretation of ACTH-beta-Endorphin Coaggregation: Relevance to Secretory Granule Biogenesis

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Title Molecular Interpretation of ACTH-beta-Endorphin Coaggregation: Relevance to Secretory Granule Biogenesis
 
Creator RANGANATHAN, S
SINGH, PK
SINGH, U
SINGRU, PS
PADINHATEERI, R
MAJI, SK
 
Subject HUMAN-DISEASE
PROTEIN
AGGREGATION
STORAGE
PEPTIDES
DYNAMICS
SIMULATIONS
AMYLOIDS
HORMONES
 
Description 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.
 
Publisher PUBLIC LIBRARY SCIENCE
 
Date 2014-10-15T12:07:30Z
2014-10-15T12:07:30Z
2012
 
Type Article
 
Identifier PLOS ONE, 7(3)
http://dx.doi.org/10.1371/journal.pone.0031924
http://dspace.library.iitb.ac.in/jspui/handle/100/14864
 
Language en