Lower Homologues of Ahpatinin, Aspartic Protease Inhibitors, from a Marine Streptomyces sp.
Lower Homologues of Ahpatinin, Aspartic Protease Inhibitors, from a Marine Streptomyces sp.
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DOI：
10.1021/np500337m
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发表时间：
2014-07-01
影响因子：
5.1
通讯作者：
Matsunaga, Shigeki
中科院分区：
文献类型：
--
作者：
Sun, Yi;Takada, Kentaro;Matsunaga, Shigeki
从一种来源于深海沉积物的链霉菌中分离出两种线性肽，ahpatinin Ac（1）和ahpatinin Pr（2），以及已知的ahpatinin Bu-i、胃酶抑素Ac、胃酶抑素Pr和胃蛋白酶链菌素。通过NMR数据的解释和转化为DNP-L-瓦尔衍生物后的水解产物的HPLC分析，对ahpatinin Pr（2）的结构进行了归属。在酸水解产物的LCMS分析期间，观察到2中他汀和Ahppa单元的逆向醇醛裂解产生的产物，并且可以促进非蛋白质氨基酸的他汀类的绝对构型的测定。ahpatinin Ac（1）和ahpatinin Pr（2）均能有效抑制胃蛋白酶，中度抑制组织蛋白酶B。
Two linear peptides, ahpatinin Ac (1) and ahpatinin Pr (2), were isolated together with the known ahpatinin Bu-i, pepstatin Ac, pepstatin Pr, and pepsinostreptin from a Streptomyces sp. derived from a deep-sea sediment. The structure of ahpatinin Pr (2) was assigned by interpretation of NMR data and HPLC analysis of the hydrolysate after converting to the DNP-L-Val derivative. During the LCMS analysis of the acid hydrolysate, products arising from the retro-aldol cleavage of the statine and Ahppa units in 2 were observed and could facilitate the determination of the absolute configuration of the statine class of nonproteinogenic amino acids. Both ahpatinin Ac (1) and ahpatinin Pr (2) potently inhibited pepsin and moderately inhibited cathepsin B.