Binding of the glycopeptide antibiotic teicoplanin to D-alanyl-D-alanine-agarose: the effect of micellar aggregates.

Binding of the glycopeptide antibiotic teicoplanin to D-alanyl-D-alanine-agarose: the effect of micellar aggregates.
复制标题

糖肽抗生素替考拉宁与 D-丙氨酰-D-丙氨酸-琼脂糖的结合:胶束聚集体的作用。

DOI:
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发表时间:
1985
期刊:
Journal of applied biochemistry
影响因子:
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通讯作者:
G. Cassani
G. Cassani
中科院分区:
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文献类型:
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作者:
A. Corti;A. Soffientini;G. Cassani

文献摘要

被引文献

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替考拉宁以及万古霉素组的其他抗生素显示与D-丙氨酰-D-丙氨酸-琼脂糖(D-Ala-D-Ala-阿加)特异性结合(A. Corti和G. Cassani,Appl. Biochem. Biotechnol. 11,101-110(1985))。这一发现被扩展,表明结合是溶液中抗生素的浓度和物理形式的函数,即,单体或胶束聚集体。在低于临界胶束浓度(CMC)的浓度下,替考拉宁的结合亲和力和能力与同组的其他抗生素(例如万古霉素和瑞斯托菌素A)相似。浓度高于CMC时,替考拉宁与D-Ala-D-Ala-阿加的结合量是其他两种抗生素的3倍。在不同pH值条件下进行的替考拉宁单体或胶束形式的平衡结合实验表明,在存在胶束的情况下,替考拉宁会发生过量结合。根据Scatchard对结合数据进行的验证表明,当替考拉宁为胶束形式时,树脂的最大结合能力增加了3.6倍。相反,表观结合亲和力较低。
Teicoplanin, as well as the other antibiotics of the vancomycin group, was shown to bind specifically to D-alanyl-D-alanine-agarose (D-Ala-D-Ala-AGA) (A. Corti and G. Cassani, Appl. Biochem. Biotechnol. 11, 101-110 (1985)). This finding is extended, showing that the binding is as a function of concentration and physical form of the antibiotic in solution, i.e., monomers or micellar aggregates. At concentrations below the critical micelle concentration (CMC) teicoplanin binds with an affinity and a capacity similar to the other antibiotics of the same group such as vancomycin and ristocetin A. At concentrations above the CMC three times more teicoplanin is bound to D-Ala-D-Ala-AGA than the other two antibiotics. Equilibrium binding experiments carried out at different pHs with teicoplanin in the monomeric or micellar form indicate that the excess binding of teicoplanin occurs in the presence of micelles. Elaboration of binding data according to Scatchard indicates that the maximum binding capacity of the resin is increased 3.6 times when teicoplanin is in the micellar form. On the contrary, the apparent binding affinity is lower.