Interaction of a synthetic antimicrobial peptide with model membrane by fluorescence spectroscopy

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorPuia Zanin, Luciana Moro
dc.creatorAlvares, Dayane dos Santos
dc.creatorJuliano, Maria Aparecida
dc.creatorPazin, Wallance Moreira
dc.creatorIto, Amando Siuiti
dc.creatorRuggiero Neto, Joo
dc.date2014-12-03T13:11:08Z
dc.date2016-10-25T20:12:16Z
dc.date2014-12-03T13:11:08Z
dc.date2016-10-25T20:12:16Z
dc.date2013-12-01
dc.date.accessioned2017-04-06T06:27:01Z
dc.date.available2017-04-06T06:27:01Z
dc.identifierEuropean Biophysics Journal With Biophysics Letters. New York: Springer, v. 42, n. 11-12, p. 819-831, 2013.
dc.identifier0175-7571
dc.identifierhttp://hdl.handle.net/11449/112901
dc.identifierhttp://acervodigital.unesp.br/handle/11449/112901
dc.identifier10.1007/s00249-013-0930-0
dc.identifierWOS:000327328300005
dc.identifierhttp://dx.doi.org/10.1007/s00249-013-0930-0
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/923655
dc.descriptionStatic and time-resolved fluorescence of tryptophan and ortho-aminobenzoic acid was used to investigate the interaction of the synthetic antimicrobial peptide L1A (IDGLKAIWKKVADLLKNT-NH2) with POPC and POPC:POPG. N-acetylated (Ac-L1A) and N-terminus covalently bonded ortho-aminobenzoic acid (Abz-L1A-W8V) were also used. Static fluorescence and quenching by acrylamide showed that the peptides adsorption to the lipid bilayers was accompanied by spectral blue shift and by a decrease in fluorescence quenching, indicating that the peptides moved to a less polar environment probably buried in the lipidic phase of the vesicles. These results also suggest that the loss of the N-terminus charge allowed deeper fluorophore insertion in the bilayer. Despite the local character of spectroscopic information, conclusions can be drawn about the peptides as a whole. The dynamic behaviors of the peptides are such that the mean intensity lifetimes, the long correlation time and the residual anisotropy at long times increased when the peptides adsorb in lipid vesicles, being larger in anionic vesicles. From the steady-state increase in fluorescence intensity and anisotropy, we observed that the partition coefficient of peptides L1A and its Abz analog in both types of vesicles are higher than the acetylated analog; moreover, the affinity to the anionic vesicle is higher than to the zwitterionic.
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.languageeng
dc.publisherSpringer
dc.relationEuropean Biophysics Journal With Biophysics Letters
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectAntimicrobial peptides
dc.subjectExtrinsically labeled peptide
dc.subjectModel membranes
dc.subjectStatic fluorescence
dc.subjectTime-resolved fluorescence
dc.titleInteraction of a synthetic antimicrobial peptide with model membrane by fluorescence spectroscopy
dc.typeOtro


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