Effects of N-terminus modifications on the conformation and permeation activities of the synthetic peptide L1A

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dc.contributor.authorMoro Zanin, Luciana Puia [UNESP]
dc.contributor.authorAraujo, Alexandre Suman de [UNESP]
dc.contributor.authorJuliano, Maria Aparecida
dc.contributor.authorCasella, Tiago
dc.contributor.authorLelles Nogueira, Mara Correa
dc.contributor.authorRuggiero Neto, Joao [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2018-11-26T16:33:10Z
dc.date.available2018-11-26T16:33:10Z
dc.date.issued2016-06-01
dc.description.abstractWe investigate the effect of the N-terminus modification of the L1A, a synthetic octadecapeptide, on its helical content, affinity and lytic action in model membranes and on its hemolytic and antibacterial activities. L1A and its acetylated analog displayed a selective antibacterial activity to Gram-negative bacteria without being hemolytic. The covalently linked 2-aminobezoic acid to the N-terminus impaired the antibacterial efficacy and increased hemolysis. Despite their lower net charge (+2), N-terminus modifications resulted in enhanced affinity and improved lytic efficiency in anionic vesicles. The analogs also showed higher helical content and consequently higher amphipathicity in these vesicles. The conformational analysis by molecular dynamics simulations in 30 % of TFE/water showed that the hydrophobic faces of the peptides are in close contact with CF3 groups of TFE while the hydrophilic faces with water molecules. Due to the loss of the amino charge, the N-termini of the analogs are buried in TFE molecules. The analysis of the pair distribution functions, obtained for the center of mass of the charged groups, has evidenced that the state of the N-terminus has influenced the possibility of different ion-pairing. The higher complexity of the bacterial cells compared with anionic vesicles hampers to establish correlations structure-function for the analogs.en
dc.description.affiliationSao Paulo State Univ, IBILCE, Dept Phys, Rua Cristovao Colombo 2265, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil
dc.description.affiliationUniv Fed Sao Paulo, Dept Byophys, Sao Paulo, Brazil
dc.description.affiliationFAMERP, Dept Dermatol Infect & Parasitary Dis, Sao Jose Do Rio Preto, SP, Brazil
dc.description.affiliationUnespSao Paulo State Univ, IBILCE, Dept Phys, Rua Cristovao Colombo 2265, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipIdFAPESP: 2010/18169-3
dc.description.sponsorshipIdFAPESP: 2011/11640-5
dc.format.extent1433-1444
dc.identifierhttp://dx.doi.org/10.1007/s00726-016-2196-1
dc.identifier.citationAmino Acids. Wien: Springer Wien, v. 48, n. 6, p. 1433-1444, 2016.
dc.identifier.doi10.1007/s00726-016-2196-1
dc.identifier.fileWOS000376609900009.pdf
dc.identifier.issn0939-4451
dc.identifier.urihttp://hdl.handle.net/11449/161541
dc.identifier.wosWOS:000376609900009
dc.language.isoeng
dc.publisherSpringer
dc.relation.ispartofAmino Acids
dc.relation.ispartofsjr1,135
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.subjectAntimicrobial peptide
dc.subjectPeptide selectivity
dc.subjectLytic activity
dc.subjectBiological activity
dc.subjectMolecular dynamics
dc.titleEffects of N-terminus modifications on the conformation and permeation activities of the synthetic peptide L1Aen
dc.typeArtigo
dcterms.licensehttp://www.springer.com/open+access/authors+rights?SGWID=0-176704-12-683201-0
dcterms.rightsHolderSpringer
unesp.author.lattes2044157599722078[2]
unesp.author.orcid0000-0002-1596-2734[4]
unesp.author.orcid0000-0001-9376-9748[2]

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Artigos - Física - IBILCE