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• W4310057000 abstract "Methicillin-resistant Staphylococcus aureus (MRSA), a biofilm-forming recalcitrant pathogen with a multidrug-resistant profile, poses a pandemic threat to human health and is the leading cause of severe infections in both healthcare and community settings. In this study, toward designing novel α-MSH-based peptides with enhanced activity and stability against MRSA, particularly its stationary phase and biofilm, we explored a design approach to augment the hydrophobicity of an 8-mer C-terminal α-MSH(6-13)-based peptide Ana-5 through the incorporation of a bulky unnatural amino acid. The designed Ana-peptides overcame the limitation of diminished activity in biological media and exhibited enhanced antistaphylococcal activity and cell selectivity. With membrane rupture as the primary mode of action, the peptides exhibited inhibitory potential against S. aureus biofilms. Importantly, the peptides did not exhibit any adverse effects in the in vivo toxicity studies and were also able to significantly alleviate bacterial infection in a systemic infection mice model study. Additionally, the peptides retained their activity in the presence of serum and displayed a low propensity toward resistance development in MRSA cells. Moreover, the observed synergistic potential of Ana-10 with conventional antibiotics could be vital in resurrecting discarded antibiotics. Thus, this study provides us with an exciting lead, Ana-10, for further development against biofilm-based chronic S. aureus infections." @default.
• W4310057000 created "2022-11-30" @default.
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• W4310057000 date "2022-11-28" @default.
• W4310057000 modified "2023-10-14" @default.
• W4310057000 title "Efficacy and Toxicity Studies of Novel α-MSH Analogues with Antibiofilm Action and β-Lactam Resensitization Potential against MRSA" @default.
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• W4310057000 doi "https://doi.org/10.1021/acsinfecdis.2c00280" @default.
• W4310057000 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36440863" @default.
• W4310057000 hasPublicationYear "2022" @default.
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