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α-螺旋型多肽HPRP-A1由15个氨基酸残基组成,来源于幽门螺杆菌核糖体蛋白L1的N端.本研究以HPRP-A1为模板,在其非极性面中心通过单个氨基酸定点取代的方法,形成一系列疏水性不同的多肽类似物,系统地研究疏水性对α-螺旋型多肽生物活性的影响.结果显示,多肽疏水性及所带净电荷对多肽生物活性起着重要的作用;HPRP-A1及疏水性相对较高的多肽类似物具有较好的广谱抗菌活性(包括革兰氏阳性菌、革兰氏阴性菌及真菌),但也有相对较高的溶血活性;多肽的疏水性与所带净电荷的变化对多肽抗细菌活性与抗真菌活性所产生的影响有着相似的变化趋势和程度.这意味着多肽与细菌的作用机制和多肽与真菌的作用机制存在一定的相关性.多肽对细菌和真菌的抗菌活性存在特异性,为设计出具有临床应用前景的抗菌肽药物奠定了基础.
The α-helical polypeptide HPRP-A1 consists of 15 amino acid residues and is derived from the N-terminus of Helicobacter pylori ribosomal protein L1.In this study, HPRP-A1 was used as a template to site-substitute a single amino acid in the center of its non- , A series of peptide analogs with different hydrophobicities were formed to systematically investigate the effect of hydrophobicity on the biological activity of α-helical polypeptides.The results showed that hydrophobicity and net charge of peptides play an important role in the biological activity of peptides ; HPRP-A1 and relatively hydrophobic peptide analogues had better broad-spectrum antibacterial activity (including Gram-positive bacteria, Gram-negative bacteria and fungi), but also had relatively high hemolytic activity; Hydrophobicity and net charge change have similar trend and degree of influence on the antimicrobial activity and antifungal activity of polypeptide, which means that the mechanism of polypeptide and bacteria and the mechanism of polypeptide and fungi are related to each other The specificity of the polypeptide for the antibacterial activity of bacteria and fungi laid the foundation for the design of antibacterial peptide drugs with clinical application prospect.