Development of highly stable galectins: Truncation of the linker peptide confers protease-resistance on tandem-repeat type galectins
Development of highly stable galectins: Truncation of the linker peptide confers protease-resistance on tandem-repeat type galectins
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DOI：
10.1016/j.febslet.2005.02.054
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发表时间：
2005-04-11
期刊：
影响因子：
3.5
通讯作者：
Nakamura, T
中科院分区：
文献类型：
--
作者：
Nishi, N;Itoh, A;Nakamura, T
半乳糖凝集素-9和半乳糖凝集素-8是β -半乳糖苷结合动物凝集素家族的成员，是治疗免疫相关疾病和肿瘤疾病的有前途的药物。该蛋白由两个由连接肽连接的碳水化合物识别结构域组成，该结构域对蛋白质水解非常敏感。为了提高蛋白酶抗性，我们通过连续截断连接肽制备突变蛋白。结果发现，缺乏整个连接肽的突变体形式对蛋白质水解具有高度稳定性，并保持其生物活性。这些突变蛋白可能是分析半乳糖凝集素-9和半乳糖凝集素-8的生物学功能和评估其治疗潜力的有用工具。(c) 2005年欧洲生化学会联合会。Elsevier B.V.版权所有。
Galectin-9 and galectin-8, members of beta-galactoside-binding animal lectin family, are promising agents for the treatment of immune-related and neoplastic diseases. The proteins consist of two carbohydrate recognition domains joined by a linker peptide, which is highly susceptible to proteolysis. To increase protease resistance, we prepared mutant proteins by serial truncation of the linker peptide. As a result, mutant forms lacking the entire linker peptide were found to be highly stable against proteolysis and retained their biological activities. These mutant proteins might be useful tools for analyzing the biological functions and evaluating the therapeutic potential of galectin-9 and galectin-8. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.