Structural and conformational analysis of hydroxycyclochlorotine and cyclochlorotine, chlorinated cyclic peptides from Penicillium islandicum.
Structural and conformational analysis of hydroxycyclochlorotine and cyclochlorotine, chlorinated cyclic peptides from Penicillium islandicum.
复制标题
羟基环氯碱和环氯碱、岛状青霉氯化环肽的结构和构象分析。
DOI：
10.1021/np800150m
复制
发表时间：
2008
影响因子：
5.1
通讯作者：
H. Morita
中科院分区：
文献类型：
--
作者：
Kohei Mizutani;Y. Hirasawa;Y. Sugita‐Konishi;N. Mochizuki;H. Morita
从岛青霉中分离到一个新的氯化环五肽羟基环氯丁(1)，并利用广泛的二维核磁共振和化学手段对1的绝对立体化学结构以及1和环氯丁(2)在DMSO-d6中的构象性质进行了分析。紫菀中的羟基环氯丁(1)和astin B(3)在残基2上均含有一个同位苏氨酸，具有顺式脯氨酸构型，而环氯丁(2)在溶液中具有两种构象状态，这可能是由脯氨酸酰胺键的顺反异构化产生的。在Ser (3)-NH和alloThr(2)的羟基氧原子之间的分子内氢键的存在可能有助于维持与顺式脯氨酸酰胺键的主构象。
A new chlorinated cyclic pentapeptide, hydroxycyclochlorotine (1), has been isolated from Penicillium islandicum, and the structure including absolute stereochemistry of 1 and conformational properties of 1 and cyclochlorotine (2) in DMSO-d6 were elucidated by using extensive 2D NMR and chemical means. Hydroxycyclochlorotine (1) and astin B (3) from Aster tataricus, each containing an allo threonine at residue 2, have a cis proline configuration, whereas cyclochlorotine (2) has two conformational states in solution, which may be produced from cis-trans isomerization of the proline amide bond. The presence of an intramolecular hydrogen bond between Ser (3)-NH and a hydroxyl oxygen atom of alloThr (2) may serve to maintain the backbone conformation with a cis proline amide bond.