CONTRIBUTION TO THE ELUCIDATION OF THE CHEMICAL STRUCTURE OF POLYMYXIN B1.
CONTRIBUTION TO THE ELUCIDATION OF THE CHEMICAL STRUCTURE OF POLYMYXIN B1.
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对阐明多粘菌素 B1 化学结构的贡献。
DOI：
10.1093/oxfordjournals.jbchem.a127998
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发表时间：
1964
影响因子：
2.7
通讯作者：
K. Tsukamoto
中科院分区：
文献类型：
--
作者：
R. Suzuki;K. Hayashi;K. Fujikawa;K. Tsukamoto
为了确定多粘菌素B1的总结构，用枯草杆菌肽酶A酶解多粘菌素B1，所得水解产物通过逆流分配进行分级。从多粘菌素B中分离出4个多肽，并测定了它们的氨基酸序列，得到了MOA→（α）L-DAB→L-Thr→（α）L-DAB和cyclo-（γ）L-DAB→（α）L-DAB →（α）L-Phe →L-Leu→（α）L-DAB→（α）L-Thr→这两个多肽，它们是阐明多粘菌素B的完整结构所必需的。因此，确定侧链连接至环肽部分中的α，γ-二氨基丁酸残基的α-氨基，并且该残基的γ-氨基参与成环，并且多粘菌素B1中存在的氨基酸除苯丙氨酸外均为L-构型。多粘菌素B1的结构为MOA→（α）L-DAB→L-Thr→（α）L-DAB→cyclo-（γ）L-DAB→（α）L-DAB→D-Phe→L-Leu→（α）L-DAB→（α）L-DAB→L-Thr→。
In order to determine the total structure, polymyxin B1has been enzymatically hydrolyzed with Subtilopeptidase A and the resulting hydrolvsate was fractionated by countercurrent distribution. Four peptides have been isolated and their amino acid sequences were determined, and the peptides, MOA→(α)L-DAB→L-Thr→(α)L-DAB and cyclo-(γ)L-DAB→(α)L-DAB→D-Phe→L-Leu→(α)L-DAB→(α)L-DAB→L-Thr→, which were essential to elucidate the full structure of polymyxin B were obtained. It was thus determined that the side chain is linked to the α-amino group of an α, γ-diaminobutyric acid residue in the cyclic peptide portion and the γ-amino group of this residue is involved in the ring formation, and that the amino acids present in polymyxin B1are contained as the L-configuration except phenylalanine. The structure of polymyxin B1was thus elucidated to be MOA→(α)L-DAB→L-Thr→(α)L-DAB→cyclo-(γ)L-DAB→(α)L-DAB→D-Phe→L-Leu→(α)L-DAB→(α)L-DAB→L-Thr→.