Unusual structural transition of antimicrobial VP1 peptide

Ganesh Shanmugam; Nsoki Phambu; Prasad L Polavarapu

doi:10.1016/j.bpc.2011.03.005

Unusual structural transition of antimicrobial VP1 peptide

Biophys Chem. 2011 May;155(2-3):104-8. doi: 10.1016/j.bpc.2011.03.005. Epub 2011 Mar 9.

Authors

Ganesh Shanmugam¹, Nsoki Phambu, Prasad L Polavarapu

Affiliation

¹ Department of Chemistry Vanderbilt University, Nashville, TN 37235, USA.

PMID: 21458141
DOI: 10.1016/j.bpc.2011.03.005

Abstract

VP1 peptide, an active domain of m-calpain enzyme with antimicrobial activity is found to undergo an unusual conformational transition in trifluoroethanol (TFE) solvent. The nature of, and time dependent variations in, circular dichroism associated with the amide I vibrations, suggest that VP1 undergoes self-aggregation forming anti-parallel β-sheet structure in TFE. Transmission electron micrograph (TEM) images revealed that β-sheet aggregates formed by VP1 possess fibril-like assemblies.

Publication types

Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Amino Acid Sequence
Circular Dichroism
Microscopy, Electron, Transmission
Molecular Sequence Data
Oligopeptides / chemistry*
Oligopeptides / genetics
Protein Structure, Secondary
Spectroscopy, Fourier Transform Infrared

Substances

Oligopeptides
glycyl-threonyl-alanyl-methionyl-arginyl-isoleucyl-leucyl-glycyl-glycyl-valyl-isoleucine