Insights into the molecular flexibility of θ-defensins by NMR relaxation analysis.

ABSTRACT: θ-Defensins are mammalian cyclic peptides that have antimicrobial activity and show potential as stable scaffolds for peptide-based drug design. The cyclic cystine ladder structural motif of θ-defensins has been characterized using NMR spectroscopy and is important for their structure and stability. However, the effect of the pronounced elongated topology of θ-defensins on their molecular motion is not yet understood. Studies of molecular motion by NMR relaxation measurements have been facilitated by the recent development of a semirecombinant method for producing cyclic peptides that allows for isotopic labeling. Here we have undertaken a multifield (15)N NMR relaxation analysis of the anti-HIV θ-defensin, HTD-2, and interpreted the experimental data using various models of overall and in

SUBMITTER: Conibear AC 

PROVIDER: S-EPMC5811197 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature