title: Unusual structural transition of antimicrobial VP1 peptide.
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.
authors: Department of Chemistry Vanderbilt University, Nashville, TN 37235, USA.
authors: Ganesh
authors: G
authors: Shanmugam
authors: Nsoki
authors: N
authors: Phambu
authors: Prasad L
authors: PL
authors: Polavarapu
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D046529:Microscopy, Electron, Transmission; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry* / Q000235:genetics; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D009842:Oligopeptides; C523526:glycyl-threonyl-alanyl-methionyl-arginyl-isoleucyl-leucyl-glycyl-glycyl-valyl-isoleucine