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Probing the Conformational Dynamics of the Bioactive Peptide TLQP ‐21 in Solution: A Molecular Dynamics Study
Author(s) -
Chakraborty Sandipan,
Akhter Shamim,
Requena Jesús R.,
Basu Soumalee
Publication year - 2015
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/cbdd.12541
Subject(s) - peptide , molecular dynamics , chemistry , biophysics , folding (dsp implementation) , peptide sequence , protein structure , stereochemistry , crystallography , biochemistry , computational chemistry , biology , electrical engineering , engineering , gene
VGF ‐derived peptide, TLQP ‐21, is a physiologically active neuropeptide exhibiting important roles in energy expenditure and balance, gastric contractility, reproduction, pain modulation, and stress. Although the physiological functions of the peptide constitute a research area of considerable interest, structural information is clearly lacking. Here, using extensive 550 nanoseconds molecular dynamics simulation in explicit water model, we have explored the folding energy landscape of the peptide. Principal component analysis and cluster analysis have been used to identify highly populated conformational states of the peptide in solution. The most populated structure of the peptide adopts a highly compact globular form stabilized by several hydrogen‐bonding interactions and π ‐cationic interactions. Strong surface complementarity of hydrophobic residues allows tighter spatial fit of the residues within the core region of the peptide. Our simulation also predicts that the peptide is highly flexible in solution and that the region A 7 ‐R 9 and three C‐terminal residues, P 19 ‐R 21 , possess strong helical propensity.