【作者】 刘雪辉； 崔育新；

【Author】 Liu Xuhui Cui Yuxin School of Pharmaceutical Sciences,State Key Laboratory of Natural and Biomimetic Drugs,Medical and Health Analysis Center,Peking University,Beijing,100083,P.R.China

【机构】 北京大学药学院,天然药物及仿生药物国家重点实验室,医药卫生分析中心；

【摘要】 <正>细胞因子是一类小分子量蛋白质,它们在免疫及炎性反应中发挥着重要的作用。趋化因子属于细胞因子的一种,体内存在多种趋化因子。在体内,它们的主要作用是募集和活化白细胞。趋化样因子1(CKLF1)对于嗜中性细胞、巨细胞及淋巴细胞有趋化活性,而该细胞更多还原

【Abstract】 Human chemokine like factor 1(CKLF1)was a recently discovered multi-functional chemokine like factor.N-terminal amino acid sequencing with secreted CKLF1 protein determined that it had at least two mature forms named C19 and C27, respectively.Recent experiments proved that C27 should be a natural agonist for CCR4,while C 19 may be an antagonist.In this study,we examined the two peptides with traditional 2D NMR methods.Results showed that,all of the two peptides adopted a flexible extended conformation.Only the three prolines seemed to mildly restrict the local region of Ser4-His 13(residue number in C 19).We deduced that this mild restriction of these prolines might play an important role in the recognition process of the C 19/C27 to CCR4.The N-terminal of C27 showed more flexibility due to lacking of the proline residues and may activate the CCR4 after the initial recognition procedure in a traditional chemokine way.Since these two peptides differed in the N-terminal region by 8 residues,the above results may hold the key information on research of the CCR4 antagonists and agonists.更多还原