- Molecular dynamics simulations of the secondary-binding site in disaccharide-modified glycopeptide antibiotics

The chemical structures of the glycopeptide antibiotics and a PG-repeat unit. (a) Chemical structure of [¹⁹F]oritavancin with the biphenyl moiety highlighted in grey. (b) Chemical structure of chloroeremomycin with the 4-epi-vancosamine highlighted in grey. (c) Chemical structure of vancomycin with the first amino acid residue, N-methylleucine (grey circle). The cleavage of the N-methylleucine from [¹⁹F]oritavancin, chloroeremomycin, and vancomycin by Edman degradation results in desleucyl-[¹⁹F]oritavancin, desleucyl-chloroeremomycin, and desleucyl-vancomycin, respectively. (d) Chemical structure of the peptide portion of the PG-repeat unit in S. aureus with amino acid sequence acyl-l-Lys(Gly5)-d-Ala-d-Ala. A pentaglycine is attached to the ɛ-nitrogen of the l-Lys. The primary-binding site of the glycopeptide antibiotics binds to the d-Ala-d-Ala of the PG-repeat unit (grey oval). The PG disaccharide N-acetylglucosamine-N-acetylmuramic acid does not participate in the binding and thus was removed from the glycopeptide–PG complex.

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Reference

Molecular dynamics simulations of the secondary-binding site in disaccharide-modified glycopeptide antibiotics - Scientific Figure on ResearchGate. Available from: https://www.researchgate.net/figure/The-chemical-structures-of-the-glycopeptide-antibiotics-and-a-PG-repeat-unit-a_fig1_360271659 [accessed 2 Jul, 2024]

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The chemical structures of the glycopeptide antibiotics and a PG-repeat unit. (a) Chemical structure of [¹⁹F]oritavancin with the biphenyl moiety highlighted in grey. (b) Chemical structure of chloroeremomycin with the 4-epi-vancosamine highlighted in grey. (c) Chemical structure of vancomycin with the first amino acid residue, N-methylleucine (grey circle). The cleavage of the N-methylleucine from [¹⁹F]oritavancin, chloroeremomycin, and vancomycin by Edman degradation results in desleucyl-[¹⁹F]oritavancin, desleucyl-chloroeremomycin, and desleucyl-vancomycin, respectively. (d) Chemical structure of the peptide portion of the PG-repeat unit in S. aureus with amino acid sequence acyl-l-Lys(Gly5)-d-Ala-d-Ala. A pentaglycine is attached to the ɛ-nitrogen of the l-Lys. The primary-binding site of the glycopeptide antibiotics binds to the d-Ala-d-Ala of the PG-repeat unit (grey oval). The PG disaccharide N-acetylglucosamine-N-acetylmuramic acid does not participate in the binding and thus was removed from the glycopeptide–PG complex.

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<a href="https://www.researchgate.net/figure/The-chemical-structures-of-the-glycopeptide-antibiotics-and-a-PG-repeat-unit-a_fig1_360271659"><img src="https://www.researchgate.net/publication/360271659/figure/fig1/AS:1150752521240582@1651372189604/The-chemical-structures-of-the-glycopeptide-antibiotics-and-a-PG-repeat-unit-a.png" alt="The chemical structures of the glycopeptide antibiotics and a PG-repeat unit. (a) Chemical structure of [¹⁹F]oritavancin with the biphenyl moiety highlighted in grey. (b) Chemical structure of chloroeremomycin with the 4-epi-vancosamine highlighted in grey. (c) Chemical structure of vancomycin with the first amino acid residue, N-methylleucine (grey circle). The cleavage of the N-methylleucine from [¹⁹F]oritavancin, chloroeremomycin, and vancomycin by Edman degradation results in desleucyl-[¹⁹F]oritavancin, desleucyl-chloroeremomycin, and desleucyl-vancomycin, respectively. (d) Chemical structure of the peptide portion of the PG-repeat unit in S. aureus with amino acid sequence acyl-l-Lys(Gly5)-d-Ala-d-Ala. A pentaglycine is attached to the ɛ-nitrogen of the l-Lys. The primary-binding site of the glycopeptide antibiotics binds to the d-Ala-d-Ala of the PG-repeat unit (grey oval). The PG disaccharide N-acetylglucosamine-N-acetylmuramic acid does not participate in the binding and thus was removed from the glycopeptide–PG complex."/></a>