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目的 对本室从人子宫颈粘液分离纯化的1个抗菌多肽HCP- 1进行分子结构特性分析。方法 分离HCP- 1多肽,测定其氮端氨基酸序列,根据其氮端氨基酸序列密码子设计简并引物,采用3′- RACE- PCR技术扩增HCP- 1编码基因,连接到T载体进行测序。用生物软件分析测序结果。结果 以简并引物结合RACE- PCR技术成功的克隆出HCP- 1全长c DNA,BL AST分析证实其序列与HMG- 17分子相同,OMIGA软件分析发现其含有一个α-螺旋结构(疏水结构区)可能是其抗菌功能的基础。结论 HCP- 1为HMG- 17,是存在于宫颈粘液抗菌的一种抗菌多肽,其中的α-螺旋结构可能是其抗菌的结构基础。
Objective To analyze the molecular structure of one antimicrobial peptide HCP-1 isolated and purified from human cervical mucus. Methods The HCP-1 polypeptide was isolated and its N-terminal amino acid sequence was determined. Degenerate primers were designed according to the N-terminal amino acid sequence codon. HCP-1 encoding gene was amplified by 3’-RACE PCR and ligated into T vector for sequencing. The sequencing results were analyzed using biological software. Results The full length cDNA of HCP-1 was successfully cloned by degenerate primers and RACE-PCR. BLAST analysis confirmed that the sequence of HCP-1 was the same as that of HMG-17. OMIGA software analysis showed that it contains an α-helical structure ) May be the basis of its antimicrobial function. Conclusion HCP-1 is HMG-17, an antimicrobial polypeptide that exists in cervical mucus antibacterial activity. The α-helical structure of HCP-1 may be the structural basis of its antimicrobial activity.