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

dc.contributorUniversidade Estadual Paulista (Unesp)
dc.creatorPuia Zanin, Luciana Moro [UNESP]
dc.creatorAlvares, Dayane dos Santos [UNESP]
dc.creatorJuliano, Maria Aparecida [UNESP]
dc.creatorPazin, Wallance Moreira [UNESP]
dc.creatorIto, Amando Siuiti [UNESP]
dc.creatorRuggiero Neto, Joo [UNESP]
dc.date2014-12-03T13:11:08Z
dc.date2014-12-03T13:11:08Z
dc.date2013-12-01
dc.date.accessioned2023-09-09T10:06:35Z
dc.date.available2023-09-09T10:06:35Z
dc.identifierhttp://dx.doi.org/10.1007/s00249-013-0930-0
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.identifier10.1007/s00249-013-0930-0
dc.identifierWOS:000327328300005
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8762519
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.descriptionINCT-FCx
dc.descriptionINCT
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.descriptionSao Paulo State Univ, Dept Phys, IBILCE, UNESP, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil
dc.descriptionSao Paulo State Univ, Dept Phys, IBILCE, UNESP, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil
dc.descriptionFAPESP: 11/11640-5
dc.descriptionFAPESP: 12/08147-8
dc.format819-831
dc.languageeng
dc.publisherSpringer
dc.relationEuropean Biophysics Journal With Biophysics Letters
dc.relation1.935
dc.relation0,604
dc.rightsAcesso restrito
dc.sourceWeb of Science
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.typeArtigo


Este ítem pertenece a la siguiente institución