Nieto M, Perkins H R
Biochem J. 1971 Oct;124(5):845-52. doi: 10.1042/bj1240845.
The affinity of ristocetin B for analogues of the C-terminal tripeptide sequence of bacterial cell wall mucopeptide precursors resembles that of vancomycin. Complex-formation requires a d-configuration in the two amino acid residues of the C-terminal dipeptide, an l-configuration is preferred in the preceding amino acid residue and positive charges on the peptide molecule decrease its affinity. The specificity of ristocetin B, however, differs from that of vancomycin in the requirements for the size of the side chains on the C-terminal dipeptide. These differences may explain the observed differences in antibiotic behaviour of vancomycin and ristocetin with particular micro-organisms. The optical rotatory dispersion and u.v.-absorption characteristics of the ristocetins are very different from those of vancomycin but nearly identical with those of ristomycin A. Aglycones prepared from ristomycin A were antibiotically active and also combined with a specific peptide.
瑞斯托菌素B对细菌细胞壁粘肽前体C末端三肽序列类似物的亲和力与万古霉素相似。形成复合物需要C末端二肽的两个氨基酸残基具有d构型，在前一个氨基酸残基中l构型更优，并且肽分子上的正电荷会降低其亲和力。然而，瑞斯托菌素B的特异性在C末端二肽侧链大小的要求方面与万古霉素不同。这些差异可能解释了观察到的万古霉素和瑞斯托菌素对特定微生物的抗生素行为差异。瑞斯托菌素的旋光色散和紫外吸收特性与万古霉素非常不同，但与瑞斯托霉素A几乎相同。从瑞斯托霉素A制备的苷元具有抗生素活性，并且也能与特定肽结合。
