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• W4382933190 endingPage "1448" @default.
• W4382933190 startingPage "1437" @default.
• W4382933190 abstract "The development of new antibiotics is urgently required because of the rapidly growing resistance against conventional antibiotics. The antimicrobial peptides show potential as small antibiotic molecules. The stability of peptides is a primary concern for the use of peptides as drugs. Introducing β-amino acids into peptide sequences can be useful in preventing biological degradation by proteolytic enzymes. Herein, we describe the synthesis, characterization, and antimicrobial activity of ultra-short cationic β-peptides, LA-β3,3-Pip-β2,2-Ac6c-PEA, P1; LA-β3,3-Pip(G)-β2,2-Ac6c-PEA, P2; LAU-β3,3-Pip-β2,2-Ac6c-PEA, P3, and LAU-β3,3-Pip(G)-β2,2-Ac6c-PEA, P4. Peptides P1–P4 were evaluated against Gram-negative, Gram-positive, MRSA, and multi-drug resistant E. coli (MDR-E. coli). P3 exhibited the most potent antimicrobial activity against E. coli, S. epidermidis, S. aureus, K. pneumoniae, S. mutans, and E. faecalis, with MIC values 0.5, 2, 0.5, 1, 2, and 1 μg/mL, respectively. P3 exhibited time- and concentration-dependent bactericidal activities against E. coli, S. aureus, and E. faecalis with a killing rate of 1.6 logs/h. The treatment of E. coli with peptide P3 showed membrane disruption. In addition, P3 exhibited the inhibition of biofilm produced by E. coli, synergism with antibiotics (ciprofloxacin, streptomycin, and ampicillin), 100% cell viability against AML12, RAW 264.7, and HEK-293 cell lines at 1, and 10 μg/mL concentrations." @default.
• W4382933190 created "2023-07-04" @default.
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• W4382933190 date "2023-07-03" @default.
• W4382933190 modified "2023-09-27" @default.
• W4382933190 title "Synthesis, Characterization, and Antimicrobial Activity of Ultra-Short Cationic β-Peptides" @default.
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• W4382933190 doi "https://doi.org/10.1021/acsinfecdis.3c00238" @default.
• W4382933190 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37399583" @default.
• W4382933190 hasPublicationYear "2023" @default.
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