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- W2019979826 abstract "The molecular target of vancomycin, a commonly used glycopeptide antibiotic, is the d-Ala-d-Ala dipeptide subunit on the bacterial cell wall. The molecular basis of interaction between vancomycin and d-Ala-d-Ala in solution is well-known. However, there is no structural data on vancomycin, and its interaction with d-Ala-d-Ala when the drug is tethered to a solid support. In this Article, vancomycin was directly coupled onto TentaGel or PEGA resin through its C terminus. High-resolution magic angle spinning NMR studies indicated that conformation of PEGA bead-bound vancomycin is identical to that of the free drug. Broadening and shifts of the same proton resonances were observed in solution-phase vancomycin or PEGA-bound vancomycin when complexed with Ac2-l-Lys-d-Ala-d-Ala. This study demonstrates that bead-bound molecules can behave the same as solution-phase molecules in terms of molecular interaction with its target molecule, thus validating the on-bead screening approach of the “one-bead−one-compound” combinatorial library method." @default.
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- W2019979826 date "2004-12-15" @default.
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- W2019979826 title "Conformational Studies of Resin-Bound Vancomycin and the Complex of Vancomycin and Ac<sub>2</sub>-<scp>l</scp>-Lys-<scp>d</scp>-Ala-<scp>d</scp>-Ala" @default.
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- W2019979826 doi "https://doi.org/10.1021/cc0498783" @default.
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