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Cited 3 time in webofscience Cited 2 time in scopus
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Identification of Bacterial Membrane Selectivity of Romo1-Derived Antimicrobial Peptide AMPR-22 via Molecular Dynamics

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dc.contributor.authorKim, Hana-
dc.contributor.authorYoo, Young Do-
dc.contributor.authorLee, Gi Young-
dc.date.accessioned2022-08-02T00:40:14Z-
dc.date.available2022-08-02T00:40:14Z-
dc.date.issued2022-07-
dc.identifier.issn1661-6596-
dc.identifier.issn1422-0067-
dc.identifier.urihttps://scholarworks.korea.ac.kr/kumedicine/handle/2021.sw.kumedicine/61231-
dc.description.abstractThe abuse or misuse of antibiotics has caused the emergence of extensively drug-resistant (XDR) bacteria, rendering most antibiotics ineffective and increasing the mortality rate of patients with bacteremia or sepsis. Antimicrobial peptides (AMPs) are proposed to overcome this problem; however, many AMPs have attenuated antimicrobial activities with hemolytic toxicity in blood. Recently, AMPR-11 and its optimized derivative, AMPR-22, were reported to be potential candidates for the treatment of sepsis with a broad spectrum of antimicrobial activity and low hemolytic toxicity. Here, we performed molecular dynamics (MD) simulations to clarify the mechanism of lower hemolytic toxicity and higher efficacy of AMPR-22 at an atomic level. We found four polar residues in AMPR-11 bound to a model mimicking the bacterial inner/outer membranes preferentially over eukaryotic plasma membrane. AMPR-22 whose polar residues were replaced by lysine showed a 2-fold enhanced binding affinity to the bacterial membrane by interacting with bacterial specific lipids (lipid A or cardiolipin) via hydrogen bonds. The MD simulations were confirmed experimentally in models that partially mimic bacteremia conditions in vitro and ex vivo. The present study demonstrates why AMPR-22 showed low hemolytic toxicity and this approach using an MD simulation would be helpful in the development of AMPs.-
dc.language영어-
dc.language.isoENG-
dc.publisherMultidisciplinary Digital Publishing Institute (MDPI)-
dc.titleIdentification of Bacterial Membrane Selectivity of Romo1-Derived Antimicrobial Peptide AMPR-22 via Molecular Dynamics-
dc.typeArticle-
dc.publisher.location스위스-
dc.identifier.doi10.3390/ijms23137404-
dc.identifier.scopusid2-s2.0-85133189919-
dc.identifier.wosid000825637400001-
dc.identifier.bibliographicCitationInternational Journal of Molecular Sciences, v.23, no.13-
dc.citation.titleInternational Journal of Molecular Sciences-
dc.citation.volume23-
dc.citation.number13-
dc.type.docTypeArticle-
dc.description.isOpenAccessY-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaChemistry-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryChemistry, Multidisciplinary-
dc.subject.keywordPlusUCSF CHIMERA-
dc.subject.keywordPlusSIMULATIONS-
dc.subject.keywordPlusMECHANISMS-
dc.subject.keywordPlusRESISTANCE-
dc.subject.keywordPlusROMO1-
dc.subject.keywordPlusGUI-
dc.subject.keywordAuthorAMPR-22-
dc.subject.keywordAuthorantimicrobial peptide-
dc.subject.keywordAuthormolecular dynamics-
dc.subject.keywordAuthorextensively drug-resistant bacteria-
dc.subject.keywordAuthorbacterial membrane selectivity-
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