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A C-terminal cationic fragment derived from an arginine-rich peptide exhibits in vitro antibacterial and anti-plasmodial activities governed by its secondary structure properties

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dc.creatorLesmes, Liliana Patriciaspa
dc.creatorBohorquez, Magda Yenithspa
dc.creatorCarreño, Luisa Fernandaspa
dc.creatorPatarroyo, Manuel Elkinspa
dc.creatorLozano, José Manuelspa
dc.date.accessioned2020-05-25T23:58:00Z
dc.date.available2020-05-25T23:58:00Z
dc.date.created2009spa
dc.description.abstractThe differential in vitro antimicrobial activity of a 12-residue-long arginine-rich peptide derived from protamine was examined against bacterial and parasite microbes. A design of discrete peptide fragments based on the thermolysin-digestion map allowed us to propose three peptide fragments to be further assessed regarding their biological and secondary structural properties. Peptide structure allowed designing three arginine-rich fragments. All peptide fragments were assessed regarding their antimicrobial activity against Gram-positive and Gram-negative bacteria and a human malaria strain. Qualitative and quantitative assays carried out for determining all peptides' antibacterial activity at different concentration levels included radial diffusion and a time-controlled technique. Tests demonstrated that all assessed molecules inhibited invasion of Plasmodium falciparum parasites to human red blood cells. Cytolytic activity of the parent protamine peptide was completely abolished by strategically fragmenting its aminoacid sequence. Remarkably, the cationic C-fragment exhibited stronger biological activity than its parent peptide. Interestingly, the peptide fragment denoted as 2077 displays a typical ?-helix profile according to its CD spectrum. The results support proposing the protamine C-terminal fragment as a potential new antimicrobial peptide. © 2009 Elsevier Inc. All rights reserved.eng
dc.format.mimetypeapplication/pdf
dc.identifier.doihttps://doi.org/10.1016/j.peptides.2009.08.011
dc.identifier.issn1969781
dc.identifier.urihttps://repository.urosario.edu.co/handle/10336/22783
dc.language.isoengspa
dc.relation.citationEndPage2160
dc.relation.citationIssueNo. 12
dc.relation.citationStartPage2150
dc.relation.citationTitlePeptides
dc.relation.citationVolumeVol. 30
dc.relation.ispartofPeptides, ISSN:1969781, Vol.30, No.12 (2009); pp. 2150-2160spa
dc.relation.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-70449631089&doi=10.1016%2fj.peptides.2009.08.011&partnerID=40&md5=e250bfe99f9e97b2124462607ab9eca2spa
dc.rights.accesRightsinfo:eu-repo/semantics/openAccess
dc.rights.accesoAbierto (Texto Completo)spa
dc.source.instnameinstname:Universidad del Rosariospa
dc.source.reponamereponame:Repositorio Institucional EdocURspa
dc.subject.keywordAmpicillinspa
dc.subject.keywordAndropinspa
dc.subject.keywordAntimicrobial peptide 2075spa
dc.subject.keywordAntimicrobial peptide 2076spa
dc.subject.keywordAntimicrobial peptide 2077spa
dc.subject.keywordAntimicrobial peptide mp 17spa
dc.subject.keywordAntimicrobial peptide mp 3spa
dc.subject.keywordAntimicrobial peptide mp 7spa
dc.subject.keywordAntimicrobial peptide mp 8spa
dc.subject.keywordAntimicrobial peptide mp xspa
dc.subject.keywordAntimicrobial peptide pglaspa
dc.subject.keywordAntimicrobial peptide tapspa
dc.subject.keywordApaminspa
dc.subject.keywordBombininspa
dc.subject.keywordCecropin aspa
dc.subject.keywordCecropin bspa
dc.subject.keywordCecropin p1spa
dc.subject.keywordCriptidinspa
dc.subject.keywordDermaseptinspa
dc.subject.keywordKanamycinspa
dc.subject.keywordMaganin 2spa
dc.subject.keywordMaganin ispa
dc.subject.keywordMelittinspa
dc.subject.keywordPolistesspa
dc.subject.keywordPolistes maspa
dc.subject.keywordPolypeptide antibiotic agentspa
dc.subject.keywordProtaminespa
dc.subject.keywordTaquilepsin 1spa
dc.subject.keywordThermolysinspa
dc.subject.keywordUnclassified drugspa
dc.subject.keywordUnindexed drugspa
dc.subject.keywordAlpha helixspa
dc.subject.keywordAmino acid sequencespa
dc.subject.keywordAntibacterial activityspa
dc.subject.keywordAntibiotic sensitivityspa
dc.subject.keywordAntiprotozoal activityspa
dc.subject.keywordArticlespa
dc.subject.keywordCarboxy terminal sequencespa
dc.subject.keywordConcentration responsespa
dc.subject.keywordControlled studyspa
dc.subject.keywordCytolysisspa
dc.subject.keywordDisk diffusionspa
dc.subject.keywordErythrocytespa
dc.subject.keywordGram negative bacteriumspa
dc.subject.keywordGram positive bacteriumspa
dc.subject.keywordHost parasite interactionspa
dc.subject.keywordHumanspa
dc.subject.keywordHuman cellspa
dc.subject.keywordIn vitro studyspa
dc.subject.keywordNonhumanspa
dc.subject.keywordPhysical chemistryspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPriority journalspa
dc.subject.keywordProtein secondary structurespa
dc.subject.keywordQualitative analysisspa
dc.subject.keywordQuantitative analysisspa
dc.subject.keywordStructure activity relationspa
dc.subject.keywordAnimalsspa
dc.subject.keywordAnti-bacterial agentsspa
dc.subject.keywordAntimalarialsspa
dc.subject.keywordAntimicrobial cationic peptidesspa
dc.subject.keywordArgininespa
dc.subject.keywordErythrocytesspa
dc.subject.keywordHumansspa
dc.subject.keywordMicrobial sensitivity testsspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordBacteria (microorganisms)spa
dc.subject.keywordNegibacteriaspa
dc.subject.keywordPlasmodium falciparumspa
dc.subject.keywordPosibacteriaspa
dc.subject.keyword?-helixspa
dc.subject.keywordAnti-plasmodial activityspa
dc.subject.keywordAntimicrobial peptidespa
dc.subject.keywordArginine-rich peptidespa
dc.subject.keywordSecondary structurespa
dc.titleA C-terminal cationic fragment derived from an arginine-rich peptide exhibits in vitro antibacterial and anti-plasmodial activities governed by its secondary structure propertiesspa
dc.typearticleeng
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersion
dc.type.spaArtículospa
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