Demonstration of the difference in binding affinity between the two binding sites of the ristocetin A asymmetric dimer

G. Batta, Michael F. Cristofaro, Gary J. Sharman, Dudley H. Williams

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

The titration of 13C labelled N-acetyl-D-ala-D-ala with the glycopeptide antibiotics ristocetin A and eremomycin, monitored by 13C NMR spectroscopy, demonstrates that the two distinct binding sites of the ristocetin A asymmetric dimer have different affinities, whereas those of eremomycin show no detectable difference.

Original languageEnglish
Pages (from-to)101-103
Number of pages3
JournalChemical Communications
Issue number1
Publication statusPublished - Jan 7 1996

Fingerprint

Antibiotics
Binding sites
Titration
Dimers
Nuclear magnetic resonance spectroscopy
Demonstrations
Binding Sites
Glycopeptides
Anti-Bacterial Agents
eremomycin
ristocetin A
alanylalanine

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Demonstration of the difference in binding affinity between the two binding sites of the ristocetin A asymmetric dimer. / Batta, G.; Cristofaro, Michael F.; Sharman, Gary J.; Williams, Dudley H.

In: Chemical Communications, No. 1, 07.01.1996, p. 101-103.

Research output: Contribution to journalArticle

Batta, G. ; Cristofaro, Michael F. ; Sharman, Gary J. ; Williams, Dudley H. / Demonstration of the difference in binding affinity between the two binding sites of the ristocetin A asymmetric dimer. In: Chemical Communications. 1996 ; No. 1. pp. 101-103.
@article{8d3c3aec26184fc18b88009f6cd4ffe5,
title = "Demonstration of the difference in binding affinity between the two binding sites of the ristocetin A asymmetric dimer",
abstract = "The titration of 13C labelled N-acetyl-D-ala-D-ala with the glycopeptide antibiotics ristocetin A and eremomycin, monitored by 13C NMR spectroscopy, demonstrates that the two distinct binding sites of the ristocetin A asymmetric dimer have different affinities, whereas those of eremomycin show no detectable difference.",
author = "G. Batta and Cristofaro, {Michael F.} and Sharman, {Gary J.} and Williams, {Dudley H.}",
year = "1996",
month = "1",
day = "7",
language = "English",
pages = "101--103",
journal = "Chemical Communications",
issn = "1359-7345",
publisher = "Royal Society of Chemistry",
number = "1",

}

TY - JOUR

T1 - Demonstration of the difference in binding affinity between the two binding sites of the ristocetin A asymmetric dimer

AU - Batta, G.

AU - Cristofaro, Michael F.

AU - Sharman, Gary J.

AU - Williams, Dudley H.

PY - 1996/1/7

Y1 - 1996/1/7

N2 - The titration of 13C labelled N-acetyl-D-ala-D-ala with the glycopeptide antibiotics ristocetin A and eremomycin, monitored by 13C NMR spectroscopy, demonstrates that the two distinct binding sites of the ristocetin A asymmetric dimer have different affinities, whereas those of eremomycin show no detectable difference.

AB - The titration of 13C labelled N-acetyl-D-ala-D-ala with the glycopeptide antibiotics ristocetin A and eremomycin, monitored by 13C NMR spectroscopy, demonstrates that the two distinct binding sites of the ristocetin A asymmetric dimer have different affinities, whereas those of eremomycin show no detectable difference.

UR - http://www.scopus.com/inward/record.url?scp=0030025267&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030025267&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0030025267

SP - 101

EP - 103

JO - Chemical Communications

JF - Chemical Communications

SN - 1359-7345

IS - 1

ER -