The free energy change of restricting a bond rotation in the binding of peptide analogues to vancomycin group antibiotics

U. Gerhard; M.S. Searle; D.H. Williams

doi:10.1016/S0960-894X(00)80670-8

The free energy change of restricting a bond rotation in the binding of peptide analogues to vancomycin group antibiotics

U. Gerhard
, M.S. Searle
, D.H. Williams

Research output: Contribution to journal › Article › peer-review

25 Citations (Scopus)

Abstract

The adverse cost in free energy of restricting an internal bond rotation in the binding of the peptide ligands N-succinyl-D-alanine and N-fumaryl-D-alanine to the antibiotic Ristocetin A, has been estimated to be 3.7 ± 0.9 kJ mol per rotor by comparison of the difference in free energies of binding measured by UV spectrometry.

Original language	English
Pages (from-to)	803-808
Number of pages	6
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	3
Issue number	5
DOIs	https://doi.org/10.1016/S0960-894X(00)80670-8
Publication status	Published - 1 Jan 1993

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10.1016/S0960-894X(00)80670-8

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title = "The free energy change of restricting a bond rotation in the binding of peptide analogues to vancomycin group antibiotics",

abstract = "The adverse cost in free energy of restricting an internal bond rotation in the binding of the peptide ligands N-succinyl-D-alanine and N-fumaryl-D-alanine to the antibiotic Ristocetin A, has been estimated to be 3.7 ± 0.9 kJ mol per rotor by comparison of the difference in free energies of binding measured by UV spectrometry.",

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AU - Gerhard, U.

AU - Searle, M.S.

AU - Williams, D.H.

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N2 - The adverse cost in free energy of restricting an internal bond rotation in the binding of the peptide ligands N-succinyl-D-alanine and N-fumaryl-D-alanine to the antibiotic Ristocetin A, has been estimated to be 3.7 ± 0.9 kJ mol per rotor by comparison of the difference in free energies of binding measured by UV spectrometry.

AB - The adverse cost in free energy of restricting an internal bond rotation in the binding of the peptide ligands N-succinyl-D-alanine and N-fumaryl-D-alanine to the antibiotic Ristocetin A, has been estimated to be 3.7 ± 0.9 kJ mol per rotor by comparison of the difference in free energies of binding measured by UV spectrometry.

UR - https://www.scopus.com/pages/publications/0027241298

U2 - 10.1016/S0960-894X(00)80670-8

DO - 10.1016/S0960-894X(00)80670-8

M3 - Article

AN - SCOPUS:0027241298

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VL - 3

SP - 803

EP - 808

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

IS - 5

ER -

The free energy change of restricting a bond rotation in the binding of peptide analogues to vancomycin group antibiotics

Abstract

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