Journal
CHEMICAL PHYSICS LETTERS
Volume 500, Issue 1-3, Pages 161-166Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.cplett.2010.09.085
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Funding
- French 'Ministere de l'Education Nationale de la Recherche et de la Technologie'
- Region Rhone-Alpes
- Centre for Nano-Optics NANOPTEC of the Universite Lyon 1
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The involvement of the tryptophan residues in the interactions of peptides or proteins with lipid membranes justifies our characterization of the interfacial properties of a synthetic tryptophan-rich peptide by a new approach using the nonlinear optic properties of this amino acid. The positively-charged peptide (KWWKWWK) at pH 8.5, alone or in the presence of a negatively-charged phospholipid monolayer, was detected at the air-water interface by combined optical Second Harmonic Generation (SHG), a nonlinear spectroscopy, and surface tension measurements. Further polarized SHG experiments showed that the short peptide was oriented at the negatively-charged phospholipid interface. (C) 2010 Elsevier B.V. All rights reserved.
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