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抗生素替考拉宁及其糖苷配基与细胞壁肽相互作用的热力学分析

Thermodynamic analysis of the interaction of the antibiotic teicoplanin and its aglycone with cell-wall peptides.

作者信息

Arriaga P, Laynez J, Menendez M, Cañada J, Garcia-Blanco F

机构信息

Instituto de Quimica-Fisica 'Rocasolano', Serrano, Madrid, Spain.

出版信息

Biochem J. 1990 Jan 1;265(1):69-77. doi: 10.1042/bj2650069.

Abstract

The thermodynamics of the interaction of the glycopeptidic antibiotic teicoplanin and its peptidic moiety with analogues of bacterial cell-wall peptides were studied by means of calorimetric and spectrophotometric techniques. The analysis of the thermodynamic data has allowed us to evaluate the contributions of the different peptide groups to the binding process. The nature of the primary binding forces is also discussed for each interacting group, on the basis of their enthalpic and entropic contribution and in connection with the detailed structural information available for these antibiotics from n.m.r. data. Similar analyses for the case of vancomycin and ristocetin are also reported.

摘要

采用量热法和分光光度法研究了糖肽类抗生素替考拉宁及其肽部分与细菌细胞壁肽类似物相互作用的热力学。对热力学数据的分析使我们能够评估不同肽基团对结合过程的贡献。根据各相互作用基团的焓和熵贡献,并结合核磁共振数据提供的这些抗生素的详细结构信息,还讨论了每个相互作用基团的主要结合力性质。还报道了万古霉素和瑞斯托菌素情况的类似分析。

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引用本文的文献

本文引用的文献

1
STRUCTURE STUDIES ON VANCOMYCIN.万古霉素的结构研究
J Med Chem. 1965 Jan;8:18-22. doi: 10.1021/jm00325a004.
2
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Biological properties of ristocetin-ps-aglycone.瑞斯托菌素-PS-苷元的生物学特性。
J Antibiot (Tokyo). 1982 Nov;35(11):1561-4. doi: 10.7164/antibiotics.35.1561.
5
Hydrophobic interactions affect hydrogen bond strengths in complexes between peptides and vancomycin or ristocetin.
Eur J Biochem. 1984 Jan 16;138(2):345-8. doi: 10.1111/j.1432-1033.1984.tb07921.x.
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Components and degradation compounds of the avoparcin complex.
J Antibiot (Tokyo). 1983 Dec;36(12):1671-82. doi: 10.7164/antibiotics.36.1671.

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