Design and modification of frog skin peptide brevinin-1GHa with enhanced antimicrobial activity on Gram-positive bacterial strains

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dc.authoridAKCAN, Muharrem/0000-0002-5208-9575
dc.contributor.authorKara, Seyda
dc.contributor.authorKurekci, Cemil
dc.contributor.authorAkcan, Muharrem
dc.date.accessioned2024-09-18T20:25:14Z
dc.date.available2024-09-18T20:25:14Z
dc.date.issued2022
dc.departmentHatay Mustafa Kemal Üniversitesien_US
dc.description.abstractNaturally occurring frog skin peptides are one of largest sources of antimicrobial peptides that have many advantages including high potency, broad spectrum of targets and low susceptibility to multiple drug-resistance bacteria. However, they also have disadvantages such as hemolytic activity, low stability and high production costs. For these reasons, various strategies have been applied to overcome these drawbacks restricting their use in clinical trials. Previously reported brevinin-1GHa (BR-1GHa) is a 24 amino acid long antimicrobial peptide isolated from Hylarana guentheri with hemolytic activity. To enhance the antimicrobial activity of this peptide and to reduce its hemolytic activity, we designed five new temporin like analogues and examined their bioactivities. Temporins are another class of frog skin peptides without hemolytic activity and shorter than brevinins. When the antimicrobial activities of new analogues were examined against a panel of microorganisms, BR-1GHa-3, in which two alanine residues in the truncated version of BR-1GHa were replaced with leucine, exhibited significantly improved antimicrobial activity against Gram-positive bacterial strains (e.g., S. aureus ATCC 29213 and E. casseliflavus ATCC 700327) with lower hemolytic activity compared to the BR-1GHa peptide. Furthermore, BR-1GHa-4 analogue, in which Gly3 was replaced with Pro, did not show any hemolytic activity except for highest (128 mu M) concentration tested and have a strong antimicrobial effect on Gram-positive bacteria (e.g., E. faecalis ATCC 51299 and B. cereus ATCC 13061).en_US
dc.description.sponsorshipKutahya Dumlupnar University Scientific Research Projects Coordination Unit [2019-18]en_US
dc.description.sponsorshipThis work was supported by a Grant from Kutahya Dumlupnar University Scientific Research Projects Coordination Unit [Project No. 2019-18].en_US
dc.identifier.doi10.1007/s00726-022-03189-7
dc.identifier.endpage1336en_US
dc.identifier.issn0939-4451
dc.identifier.issn1438-2199
dc.identifier.issue9en_US
dc.identifier.pmid35852614en_US
dc.identifier.scopus2-s2.0-85134479576en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage1327en_US
dc.identifier.urihttps://doi.org/10.1007/s00726-022-03189-7
dc.identifier.urihttps://hdl.handle.net/20.500.12483/10180
dc.identifier.volume54en_US
dc.identifier.wosWOS:000827403000001en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherSpringer Wienen_US
dc.relation.ispartofAmino Acidsen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectFrog skin peptidesen_US
dc.subjectSolid-phase peptide synthesisen_US
dc.subjectAntimicrobial activityen_US
dc.subjectHemolytic activityen_US
dc.subjectStructure-activity relationshipsen_US
dc.titleDesign and modification of frog skin peptide brevinin-1GHa with enhanced antimicrobial activity on Gram-positive bacterial strainsen_US
dc.typeArticleen_US

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