Synthesis and antibacterial activity of nisin‐containing block copolymers

Joshi, Pranav; McGuire, Joseph; Neff, J. A.

doi:10.1002/jbm.b.31381

Cited by 29 publications

(29 citation statements)

References 38 publications

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“…Semisynthetic analogues of lantibiotics have been produced by chemically modifying lantibiotics (43,44). The most common chemical modification of lantibiotics is through reactions with a free C-terminal carboxyl group.…”

Section: Discussionmentioning

confidence: 99%

Carboxyl Analogue of Mutacin 1140, a Scaffold for Lead Antibacterial Discovery

Escano

Ravichandran

Salamat

et al. 2017

Appl Environ Microbiol

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Mutacin 1140 belongs to the epidermin group of lantibiotics. Epidermin class lantibiotics are ribosomally synthesized and posttranslationally modified antibiotics with potent activity against Gram-positive bacteria. In particular, this class is effective at targeting drug-resistant Streptococcus pneumoniae, methicillin-resistant Staphylococcus aureus (MRSA), Mycobacterium tuberculosis, and Clostridium difficile.residue is derived from a decarboxylation of a terminal cysteine that is involved in lanthionine ring formation. Studies on mutacin 1140 have revealed new insight into the structural importance of the C-terminal AviCys residue. A C-terminal carboxyl analogue of mutacin 1140 was engineered. Capping the C-terminal carboxyl group with a primary amine restores bioactivity and affords a novel opportunity to synthesize new analogues. A C-terminal fluorescein-labeled mutacin 1140 analogue traps lipid II into a large lipid II lantibiotic complex, similar to that observed in vivo for the lantibiotic nisin. A C-terminal carboxyl analogue of mutacin 1140 competitively inhibits the activity of native mutacin 1140 and nisin. The presence of a C-terminal carboxyl group prevents the formation of the large lipid II lantibiotic complexes but does not prevent the binding of the lantibiotic to lipid II. IMPORTANCE This study addressed the importance of the C-terminal S-[(Z)-2-aminovinyl]-D-cysteine (AviCys) residue for antibacterial activity. We have learned that the posttranslational modification for making the AviCys residue is presumably important for the lateral assembly mechanism of activity that traps lipid II into a large complex. The C-terminal carboxyl analogue of this class of lantibiotics is agreeable to the addition of a wide variety of substrates. The addition of fluorescein enabled in vivo visualization of the epidermin class of lantibiotics in action. These results are significant because, as we demonstrate, the presence of the AviCys residue is not essential for bioactivity, but, more importantly, the removal of the carboxyl group is essential. The ability to make a C-terminal carboxyl analogue that is modifiable will facilitate the synthesis of novel analogues of the epidermin class of lantibiotics that can be developed for new applications.KEYWORDS lantibiotic, decarboxylation, mutacin 1140, nisin L antibiotics, or lanthionine-containing antibiotics, are characterized by their posttranslational modifications (PTMs) (1). Dehydrations of serine and threonine residues into dehydroalanine and dehydrobutyrine residues, respectively, are a common modification found in lantibiotics. These dehydrated residues can be cyclized with cysteines to form thioether bridges, which are called lanthionines (2, 3). The unmodified lantibiotic is encoded by the gene lanA. The genes for biosynthesis and regulation are generally grouped together in a biosynthetic gene cluster. In class I lantibiotics, dehydrations are carried out by the dehydratase, LanB. Lanthionine ring formation is catalyzed by LanC. Lantibiotics can ...

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Section: Discussionmentioning

confidence: 99%

Carboxyl Analogue of Mutacin 1140, a Scaffold for Lead Antibacterial Discovery

Escano

Ravichandran

Salamat

et al. 2017

Appl Environ Microbiol

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“…immobilized cecropin-MEL hybrid peptide on a variety of different types of substrates such as amidated polymer brushes, hydrogel and beads [104]; nisin-tethered on block copolymers made of ethylene oxide and propylene oxide monomers [105]; cellulose membranes covered with short bactenecins analogs (Bac2A) [106]; a synthetic -helical CAP, namely E14LKK…”

Section: Particular Properties Of Rw-rich Hexapeptidesmentioning

confidence: 99%

“…Recent strategies for the immobilization of CAPs on solid surfaces used either: (i) covalent linkage via SPPS [101,106,108,116], thioalkylation [102,104,111], EDC/NHS activation on COOH-enriched surfaces [103,107], disulfide exchange reaction on polymers using thiolated-peptides [105], or (ii) non-covalent methods using highly specific interactions, such as the biotin-streptavidin system [106]. CAPs may be tethered randomly on the solid surfaces or specifically at the C terminus, N terminus or side-chains of the peptides via the -amino group of selected K residues present within the peptide sequences.…”

Section: Peptide-based Biofilmmentioning

confidence: 99%

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Cationic Antimicrobial Peptides

Phoenix

Dennison

Harris

2013

Antimicrobial Peptides

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“…The graphical representation of data (Figure 6) clearly shows the extent of microbial inhibition exhibited by different functionalized SBS polymers. The microbial concentration was determined by measuring the optical density of the broth [19][20][21] at 600 nm after 24 h, the decrease in the optical density is directly proportional to effectiveness of microbial inhibition.…”

Section: Antimicrobial Activitymentioning

confidence: 99%

Biodegradation of Styrene-Butadiene-Styrene Coploymer via Sugars Attached to the Polymer Chain

Singh¹,

Gupta²,

Adsul³

et al. 2013

AMPC

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A synthetic method was developed to chemically attach few molecules of simple sugars like glucose, mannose, galactose, maltose and xylose (0.09 -0.37 wt%) and with quaternary nitrogen pendants (0.42 -0.46 atomic%) along the polybutadiene section of polystyrene-block-polybutadiene-block-polystyrene (SBS) block copolymer. These functionalized SBS copolymers were evaluated for biodegradation using the fungal culture Aspergillus niger NCIM 1025 (ATCC 9642) and bacterial culture Pseudomonas sp. NCIM 2220, and for antimicrobial properties using bacteria E. coli DH5α and Bacillus subtilis and yeasts Pichia stipitis NCIM 3497 and P. stipitis NCIM 3499. It was conclusively demonstrated that these modified SBS block copolymers were significantly more biodegradable than the unmodified SBS; the observed weight loss after biodegradation was ~4 -14-fold for bacterial and ~7 -36-fold for fungal cultures with respect to the sugar content of modified SBS. Preliminary studies on antimicrobial properties of these biodegradable polymers showed a 4% -24% decrease in growth of the microorganisms E. coli and Bacillus subtilis studied.

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Synthesis and antibacterial activity of nisin‐containing block copolymers

Cited by 29 publications

References 38 publications

Carboxyl Analogue of Mutacin 1140, a Scaffold for Lead Antibacterial Discovery

Carboxyl Analogue of Mutacin 1140, a Scaffold for Lead Antibacterial Discovery

Cationic Antimicrobial Peptides

Biodegradation of Styrene-Butadiene-Styrene Coploymer via Sugars Attached to the Polymer Chain

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