【摘 要】
:
In general,particular combinations with disulfide bonding in cysteine-containing peptides are critical for expressing their intrinsic biological activities.In the case of human α-and β-defensins,howev
【机 构】
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Osaka University Peptide Institute, Inc.Japan
【出 处】
:
2008中国深圳蛋白质和多肽科学大会
论文部分内容阅读
In general,particular combinations with disulfide bonding in cysteine-containing peptides are critical for expressing their intrinsic biological activities.In the case of human α-and β-defensins,however,disulfide isomers without the native pairing were demonstrated to exhibit similar antimicrobial activity to that of the native defensins.Therefore,to assess the biological activities of defensins and defensin-based therapeutics,extreme care is required in the chemical synthesis to avoid ambiguity in quality.We synthesized human α-defensins 1-5 and human β-defensins 1-4 by employing Boc chemistry,and determined the optimal conditions for folding the respective reduced peptides preferentially into a native conformation.
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