Insight into the environment of tryptophan in a hydrophobic model peptide upon aggregation and interaction with lipid vesicles: a steady state and time resolved fluorescence study.

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dc.contributor.authorJoseph, Men_US
dc.contributor.authorNagaraj, Ren_US
dc.date.accessioned1998-04-01en_US
dc.date.accessioned2009-05-27T09:02:30Z
dc.date.available1998-04-01en_US
dc.date.available2009-05-27T09:02:30Z
dc.date.issued1998-04-01en_US
dc.description.abstractFluorescence spectroscopy is extensively used to monitor binding of peptides to lipid vesicles as well as orientation in the lipid bilayer. In steady-state fluorescence, the emission characteristics of intrinsic and extrinsic fluorophores, which are sensitive to environment are monitored. Life time measurements should yield useful information about the location and flexibility of fluorophores, as these factors have a significant effect on the life times. However, studies on protein structure and dynamics indicate that interpretation of life-time data is complicated (Beechem. J.M. and Brand, L. (1985) Annu. Rev. Biochem. 54, 43-71). Hence, simple well-defined systems should help in interpretation of life time data, especially in lipid-peptide interactions. In order to examine how fluorescence characteristics of tryptophan and anthroyl group would reflect molecular details of peptide aggregation and lipid-peptide interaction, studies have been carried out on a model hydrophobic peptide and its fatty acylated derivative. Steady-state fluorescence measurements suggest that: (1) the fatty acyl chain attached to an amino acid associates with the peptide chain in aqueous environment. (2) In the lipid bilayer, the acyl chain is oriented perpendicular to the lipid bilayer surface with the peptide chain at an angle to it. Analysis of the fluorescence decay of tryptophan indicates the predominance of a very short life-time component (<1ns) in aqueous environment and lipid-vesicles. Since the preexponentials were not negative, it is unlikely that this is due to extensive deactivation process. We attribute the observation of the low life time component to predominance of one rotamer around (C alpha-C beta)bond of tryptophan in aqueous and lipid environments. Our investigations suggest that fluorescence life time data need to be complemented with steady state measurements to get an insight into details of lipid-peptide interaction.en_US
dc.description.affiliationCentre for Cellular and Molecular Biology, Hyderabad, India.en_US
dc.identifier.citationJoseph M, Nagaraj R. Insight into the environment of tryptophan in a hydrophobic model peptide upon aggregation and interaction with lipid vesicles: a steady state and time resolved fluorescence study. Indian Journal of Biochemistry & Biophysics. 1998 Apr; 35(2): 67-75en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/26257
dc.language.isoengen_US
dc.source.urihttps://https://www.niscair.res.in/ScienceCommunication/ResearchJournals/rejour/ijbb/ijbb0.aspen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshLipid Bilayers --chemistryen_US
dc.subject.meshOligopeptides --chemical synthesisen_US
dc.subject.meshPhosphatidylcholines --chemistryen_US
dc.subject.meshProtein Conformationen_US
dc.subject.meshSpectrometry, Fluorescence --methodsen_US
dc.subject.meshTryptophan --chemistryen_US
dc.titleInsight into the environment of tryptophan in a hydrophobic model peptide upon aggregation and interaction with lipid vesicles: a steady state and time resolved fluorescence study.en_US
dc.typeJournal Articleen_US
dc.typeResearch Support, Non-U.S. Gov'ten_US
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