Identification of an inter-cysteine loop potentially involved in the activity of Opisthorchis viverrini-granulin-1

R. Takjoo, David T. Wilson, P. Bansal, A. Loukas, M. Smout, N. Daly
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Abstract

Aim: Identification of small bioactive regions in proteins and peptides can be useful information in drug design studies. The current study has shown that an inter-cysteine loop of the N-terminal domain of Opisthorchis viverrini granulin-1 (Ov-GRN-1), a granulin protein from the flatworm liver fluke Opisthorchis viverrini which has potent wound healing properties, maintains the bioactivity of the full-length protein. Methods: Peptides corresponding to the three inter-cysteine loops of the N-terminal domain were produced using synthetic chemistry, and their structures and bioactivities were analyzed using nuclear magnetic resonance (NMR) spectroscopy and cell proliferation assays, respectively. Results: As expected for such small peptides, NMR analysis indicated that the peptides were poorly structured in solution. However, a seven-residue peptide corresponding to loop 2 (GRN-L2) promoted cell proliferation, in contrast to the other fragments. Conclusions: The results from the current study suggest that GRN-L2 might be responsible, in part, for the bioactivity of Ov-GRN-1, and might be a useful lead molecule for subsequent wound healing studies.
半胱氨酸间环的鉴定可能参与了蛇胸菌颗粒蛋白-1的活性
目的:鉴定蛋白质和多肽中的小生物活性区域可以为药物设计研究提供有用的信息。目前的研究表明,来自扁平虫肝吸虫的颗粒蛋白Opisthorchis viverrini granulin-1 (Ov-GRN-1)的n端结构域的半胱氨酸间环维持了全长蛋白的生物活性,该蛋白具有强大的伤口愈合特性。方法:采用合成化学方法制备与n端结构域3个半胱氨酸间环对应的多肽,分别采用核磁共振(NMR)和细胞增殖实验对其结构和生物活性进行分析。结果:正如预期的那样,核磁共振分析表明这种小肽在溶液中结构不良。然而,与其他片段相比,环2对应的七残基肽(GRN-L2)促进了细胞增殖。结论:目前的研究结果表明,GRN-L2可能是Ov-GRN-1生物活性的部分原因,可能是后续伤口愈合研究中有用的先导分子。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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