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