dc.contributor.authorMohanram, Harini
dc.contributor.authorBhattacharjya, Surajit
dc.date.accessioned2014-06-03T04:35:18Z
dc.date.available2014-06-03T04:35:18Z
dc.date.copyright2014en_US
dc.date.issued2014
dc.identifier.citationMohanram, H., & Bhattacharjya, S. (2014). β-Boomerang Antimicrobial and Antiendotoxic Peptides: Lipidation and Disulfide Bond Effects on Activity and Structure. Pharmaceuticals, 7(4), 482-501.en_US
dc.identifier.issn1424-8247en_US
dc.identifier.urihttp://hdl.handle.net/10220/19528
dc.description.abstractDrug-resistant Gram-negative bacterial pathogens and endotoxin- or lipopolysaccharide (LPS)-mediated inflammations are among some of the most prominent health issues globally. Antimicrobial peptides (AMPs) are eminent molecules that can kill drug-resistant strains and neutralize LPS toxicity. LPS, the outer layer of the outer membrane of Gram-negative bacteria safeguards cell integrity against hydrophobic compounds, including antibiotics and AMPs. Apart from maintaining structural integrity, LPS, when released into the blood stream, also induces inflammatory pathways leading to septic shock. In previous works, we have reported the de novo design of a set of 12-amino acid long cationic/hydrophobic peptides for LPS binding and activity. These peptides adopt β-boomerang like conformations in complex with LPS. Structure-activity studies demonstrated some critical features of the β-boomerang scaffold that may be utilized for the further development of potent analogs. In this work, β-boomerang lipopeptides were designed and structure-activity correlation studies were carried out. These lipopeptides were homo-dimerized through a disulfide bridge to stabilize conformations and for improved activity. The designed peptides exhibited potent antibacterial activity and efficiently neutralized LPS toxicity under in vitro assays. NMR structure of C4YI13C in aqueous solution demonstrated the conserved folding of the lipopeptide with a boomerang aromatic lock stabilized with disulfide bond at the C-terminus and acylation at the N-terminus. These lipo-peptides displaying bacterial sterilization and low hemolytic activity may be useful for future applications as antimicrobial and antiendotoxin molecules.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesPharmaceuticalsen_US
dc.rights© 2014 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).en_US
dc.subjectDRNTU::Science::Medicine::Pharmacy::Pharmaceutical technology
dc.titleβ-Boomerang antimicrobial and antiendotoxic peptides : lipidation and disulfide bond effects on activity and structureen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.3390/ph7040482
dc.description.versionPublished versionen_US


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