Unusual structural transition of antimicrobial VP1 peptide

descriptionPublicationkeyboard_double_arrow_right Article 01 May 2011 English Publisher:Elsevier BVJournal:Biophysical Chemistry, volume 155, pages 104-108 (issn: 0301-4622,

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Authors: Ganesh, Shanmugam; Nsoki, Phambu; Prasad L, Polavarapu;

doi: 10.1016/j.bpc.2011.03.005

pmid: 21458141

Unusual structural transition of antimicrobial VP1 peptide

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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.

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Keywords

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

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