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Atul Rawat and Dinesh Kumar NMR investigations of structural and dynamics features of natively unstructured drug peptide – salmon calcitonin: implication to rational design of potent sCT analogs Journal of Peptide Science 19

Version of Record online: 4 DEC 2012 | DOI: 10.1002/psc.2471

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The structural and backbone dynamics features of drug peptide salmon calcitonin have been investigated in aqueous solution and have been found to be correlated very well with the functionality of the hormone. As depicted here, the helical sampling by the peptide and significant amount of conformational plasticity towards N-terminal part of the chain may be a reflection of the biologically active state. Further, the peptide in solution exhibits multiple conformational states that in turn may inhibit symmetric self-association of the peptide and thus may account for its reduced aggregation propensity compared with human calcitonin (which lacks this property).

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