ArticleScientific reports2016
Branched Peptide, B2088, Disrupts the Supramolecular Organization of Lipopolysaccharides and Sensitizes the Gram-negative Bacteria.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Complementary Activities of Host Defence Peptides and Antibiotics in Combating Antimicrobial Resistant Bacteria.Antibiotics (Basel, Switzerland) · 2023Review
- In Vivo Evaluation of ECP Peptide Analogues for the Treatment ofBiomedicines · 2022Article
- Host Defense Peptides at the Ocular Surface: Roles in Health and Major Diseases, and Therapeutic Potentials.Frontiers in medicine · 2022Review
- Hybrid derivative of cathelicidin and human beta defensin-2 against Gram-positive bacteria: A novel approach for the treatment of bacterial keratitis.Scientific reports · 2021Article
- Interest of Homodialkyl Neamine Derivatives against ResistantInternational journal of molecular sciences · 2021Article
- Molecular engineering of antimicrobial peptides: microbial targets, peptide motifs and translation opportunities.Biophysical reviews · 2021Review
- Evaluation of Host Defense Peptide (CaD23)-Antibiotic Interaction and Mechanism of Action: Insights From Experimental and Molecular Dynamics Simulations Studies.Frontiers in pharmacology · 2021Article
- Double-Headed Cationic Lipopeptides: An Emerging Class of Antimicrobials.International journal of molecular sciences · 2020Article
- An Update on Antimicrobial Peptides (AMPs) and Their Delivery Strategies for Wound Infections.Pharmaceutics · 2020Review
- Strategies in Translating the Therapeutic Potentials of Host Defense Peptides.Frontiers in immunology · 2020Review
- Decreased expression of microRNA-30b promotes the development of pulpitis by upregulating the expression of interleukin-6 receptor.Experimental and therapeutic medicine · 2019Article
- Mygalin: An Acylpolyamine With Bactericidal Activity.Frontiers in microbiology · 2019Article
- Membrane Active Antimicrobial Peptides: Translating Mechanistic Insights to Design.Frontiers in neuroscience · 2017Review
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Authors and funding
18 authors.
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Abstract
Dissecting the complexities of branched peptide-lipopolysaccharides (LPS) interactions provide rationale for the development of non-cytotoxic antibiotic adjuvants. Using various biophysical methods, we show that the branched peptide, B2088, binds to lipid A and disrupts the supramolecular organization of LPS. The disruption of outer membrane in an intact bacterium was demonstrated by fluorescence spectroscopy and checkerboard assays, the latter confirming strong to moderate synergism between B2088 and various classes of antibiotics. The potency of synergistic combinations of B2088 and antibiotics was further established by time-kill kinetics, mammalian cell culture infections model and in vivo model of bacterial keratitis. Importantly, B2088 did not show any cytotoxicity to corneal epithelial cells for at least 96 h continuous exposure or hemolytic activity even at 20 mg/ml. Peptide congeners containing norvaline, phenylalanine and tyrosine (instead of valine in B2088) displayed better synergism compared to other substitutions. We propose that high affinity and subsequent disruption of the supramolecular assembly of LPS by the branched peptides are vital for the development of non-cytotoxic antibiotic adjuvants that can enhance the accessibility of conventional antibiotics to the intracellular targets, decrease the antibiotic consumption and holds promise in averting antibiotic resistance.
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