Joint National Laboratory for Antibody Drug Engineering, Institute of Biomedical Informatics, school of Basic Medical Sciences, Henan University, Kaifeng 475004, China.
State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China.
Molecules. 2020 Jan 23;25(3):485. doi: 10.3390/molecules25030485.
W18, isolated from contaminated soil, was found to exert antimicrobial activity against Mycobacterium species, including , an important human pathogen. Here, the anti-mycobacterial compound produced by W18 was purified by a combination of hydrophobic interaction chromatography, cation exchange chromatography, and reverse phase HPLC. Active compounds from W18 were identified as a natural peptide named pantocin wh-1 with a 1927 Da molecular weight. The primary structure of this compound was detected by N-terminal amino acid sequencing. The amino acid sequence of pantocin wh-1 consisted of 16 amino acid residues with a cyclic structure. The pantocin wh-1 could be inactivated by protease K, but was heat stable and unaffected by pH (2-12). However, the activity was not completely inactivated by trypsin and pepsin. This is the first report of a cyclic polypeptide purified from a strain of .
W18 从污染土壤中分离出来，被发现对包括分枝杆菌属在内的多种微生物具有抗菌活性，分枝杆菌属是一种重要的人类病原体。在此，通过疏水性相互作用色谱、阳离子交换色谱和反相高效液相色谱的组合，对 W18 产生的抗分枝杆菌化合物进行了纯化。从 W18 中分离出的活性化合物被鉴定为一种名为 pantocin wh-1 的天然肽，分子量为 1927Da。通过 N 端氨基酸测序检测到该化合物的一级结构。pantocin wh-1 的氨基酸序列由 16 个氨基酸残基组成，具有环状结构。pantocin wh-1 可被蛋白酶 K 失活，但热稳定且不受 pH 值（2-12）影响。然而，其活性并未被胰蛋白酶和胃蛋白酶完全失活。这是首次从 菌株中纯化出环状多肽的报道。
