2018
DOI: 10.1016/bs.apcsb.2018.03.004
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Linear Analogues of the Lipopeptide Battacin With Potent In Vitro Activity Against S. aureus

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Cited by 4 publications
(3 citation statements)
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“…The antibacterial activity results showed that Compound 4 has relative activities against both gram-positive bacteria ( B. subtilis ATCC 21332) and gram-negative bacteria ( E. coli CGMCC 1.1521), which is consistent with the fact that lipopeptides (LPs) have a broad spectrum of antimicrobial activity against a variety of pathogens [ 74 ]. Although the activity of LPs against gram-positive S. aureus has been previously reported [ 75 ], in our study, the new linear lipopeptide showed no activity against S. aureus . In addition, lipopeptide(s) (LPs) produced by different microorganisms are also known for their efficient drug(s) against cancer [ 76 ].…”
Section: Discussioncontrasting
confidence: 74%
“…The antibacterial activity results showed that Compound 4 has relative activities against both gram-positive bacteria ( B. subtilis ATCC 21332) and gram-negative bacteria ( E. coli CGMCC 1.1521), which is consistent with the fact that lipopeptides (LPs) have a broad spectrum of antimicrobial activity against a variety of pathogens [ 74 ]. Although the activity of LPs against gram-positive S. aureus has been previously reported [ 75 ], in our study, the new linear lipopeptide showed no activity against S. aureus . In addition, lipopeptide(s) (LPs) produced by different microorganisms are also known for their efficient drug(s) against cancer [ 76 ].…”
Section: Discussioncontrasting
confidence: 74%
“…Studies on the cyclic peptide somatostatin yielded analogues with up to 10% improved oral bioavailability when Nmethylated at certain points (Biron et al 2008). While Nterminal acylation reduces the overall charge of the peptide, it improves proteolytic stability depending on the sequence and may also drastically improve antimicrobial activity of AMPs or grant activity to inactive sequences (Malina and Shai 2005;Radzishevsky et al 2005;Glossop et al 2018). Amidation is a common C-terminal modification employed to improve the antimicrobial potency of peptides in two ways, by increasing the net charge of the peptide and by enhancing proteolytic stability, thus improving half-life times in vivo (Stromstedt et al 2009;Kumar et al 2014;Mura et al 2016).…”
Section: Non-proteinogenic Amino Acids and Peptide Terminimentioning
confidence: 99%
“…There are several examples of inactive peptides that gained antimicrobial activity upon conjugation of a hydrophobic acyl group (Malina and Shai 2005). Structure-activity studies were conducted by generating lipopeptides of varying fatty acid lengths (Nasompag et al 2015;Glossop et al 2018). Over improving lipid membrane insertion, fatty acid conjugation may enhance secondary structure characteristics: magainin-2 analogues showed tuneable helical, β-sheet, and oligomeric conformations depending on the size of attached fatty acid, from heptanoyl to palmitoyl in length (Avrahami and Shai 2002).…”
Section: Lipopeptide Motifs and Antimicrobial Activitymentioning
confidence: 99%