Structural plasticity of the feline leukaemia virus fusion peptide: a circular dichroism study

Autor: Nicholas C. Price, Jeremy P. Bradshaw, Sharon M. Kelly, Sarah M.A. Davies
Rok vydání: 1998
Předmět:
Circular dichroism
Peptide Fragments/chemistry
Propanols
Stereochemistry
Leukemia Virus
Feline/chemistry
Lipid Bilayers
Molecular Sequence Data
Molecular Conformation
Biophysics
Peptide
Membrane Fusion
Biochemistry
Feline leukemia virus
Protein Structure
Secondary
Viral Proteins
Fusion peptide
Structural Biology
Solvents/pharmacology
Electron microscopy
Genetics
Animals
Lipid bilayer
Polytetrafluoroethylene
Molecular Biology
Protein secondary structure
Structural plasticity
chemistry.chemical_classification
Aqueous solution
biology
Chemistry
Leukemia Virus
Feline
Circular Dichroism
Sodium Dodecyl Sulfate
Lipid bilayer fusion
Cell Biology
biology.organism_classification
Peptide Fragments
Random coil
Microscopy
Electron
Spectrophotometry
Lipid Bilayers/metabolism
Solvents
Cats
Membrane Fusion/physiology
Zdroj: Davies, S M A, Kelly, S M, Price, N C & Bradshaw, J P 1998, ' Structural plasticity of the feline leukaemia virus fusion peptide: a circular dichroism study ', FEBS Letters, vol. 425, no. 3, pp. 415-418 . https://doi.org/10.1016/S0014-5793(98)00274-9
ISSN: 0014-5793
DOI: 10.1016/s0014-5793(98)00274-9
Popis: The secondary structure of the feline leukaemia virus (FeLV) fusion peptide was investigated using circular dichroism (CD), Our results show that this peptide can readily flip between random, alpha-helical and beta-sheet conformations, depending upon its environment. The CD spectrum changes from one characteristic of random coil to predominantly beta-sheet type, and finally to that showing the characteristics of alpha-helical structure on moving from an aqueous solvent, through several increasingly hydrophobic systems, to a highly hydrophobic solvent. Electron microscopy confirmed the presence of beta structure, We propose that the structural plasticity demonstrated here is crucial to the ability of the fusion peptide to perturb lipid bilayers, and thus promote membrane fusion. (C) 1998 Federation of European Biochemical Societies.
Databáze: OpenAIRE
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