Solubilization of V-ATPase transmembrane peptides by amphipol A8-35

Two transmembrane peptides encompassing the seventh transmembrane section of subunit a from V‐ATPase from Saccharomyces cerevisiae were studied as complexes with APols A8‐35 by CD and fluorescence spectroscopy, with the goal to use APols to provide a membrane‐mimicking environment for the peptides....

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Bibliographic Details
Published in:Journal of peptide science 2008-04, Vol.14 (4), p.389-393
Main Authors: Duarte, Afonso M. S., Wolfs, Cor J. A. M., Koehorst, Rob B. M., Popot, Jean-Luc, Hemminga, Marcus A.
Format: Article
Language:English
Subjects:
a8-35
Amino Acid Sequence
amphipathic polymers
amphipols
Circular Dichroism
conformation
fluorescence
integral membrane-proteins
membrane-mimicking solvents
Micelles
mimicking
Molecular Sequence Data
Molecular Weight
Peptide Fragments - chemistry
peptides
Polymers - chemistry
Polytetrafluoroethylene - chemistry
Propylamines - chemistry
Protein Conformation
Protein Structure, Secondary
proton translocation channel
Protons
Saccharomyces cerevisiae
Saccharomyces cerevisiae - enzymology
secondary structure
segment
Solubility
Solvents - chemistry
Spectrometry, Fluorescence
Tryptophan - chemistry
Vacuolar Proton-Translocating ATPases - chemistry
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Summary:Two transmembrane peptides encompassing the seventh transmembrane section of subunit a from V‐ATPase from Saccharomyces cerevisiae were studied as complexes with APols A8‐35 by CD and fluorescence spectroscopy, with the goal to use APols to provide a membrane‐mimicking environment for the peptides. CD spectroscopy was used to obtain the overall secondary structure of the peptides, whereas fluorescence spectroscopy provided information about the local environment of their tryptophan residues. The fluorescence results indicate that both peptides are trapped by APols and the CD results that they adopt a β‐sheet conformation. This result is in contrast with previous work that showed that the same peptides are α‐helical in SDS micelles and organic solvents. These observations are discussed in the context of APol physical–chemical properties and transmembrane peptide structural propensity. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.
ISSN:1075-2617
1099-1387
DOI:10.1002/psc.996