一种新的噬菌体展示载体,用于选择目标特异性肽。

IF 2.6 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Alex Chang, Joey P Ting, Alfonso Espada, Howard Broughton, Manuel Molina-Martin, Sepideh Afshar
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引用次数: 4

摘要

多肽在噬菌体上固有的低显示水平是利用噬菌体显示技术成功分离靶特异性结合物的基础和限制障碍。为了克服这一挑战,我们利用33型噬菌体载体优化了在噬菌体表面显示的肽的拷贝数。我们随机选取野生型PIII的前67个氨基酸,以确定导致其表达降低的突变体。因此,由于合成的piii肽融合蛋白在噬菌体表面的掺入量更高,显示水平提高了30倍。利用这种新型噬菌体载体将为发现治疗性肽提供坚实的基础。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
A novel phage display vector for selection of target-specific peptides.

Intrinsic low display level of polypeptides on phage is a fundamental and limiting hurdle in successful isolation of target-specific binders by phage display technology. To circumvent this challenge, we optimized the copy number of peptides displayed on the phage surface using type 33 phage vector. We randomized the first 67 amino acids of the wild type PIII to identify mutants that would result in its reduced expression. Consequently, the display level was improved by 30-fold due to higher incorporation of the synthetic PIII-peptide fusion protein on the phage surface. Utilization of this novel phage vector should provide a solid basis for the discovery of therapeutic peptides.

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来源期刊
Protein Engineering Design & Selection
Protein Engineering Design & Selection 生物-生化与分子生物学
CiteScore
3.30
自引率
4.20%
发文量
14
审稿时长
6-12 weeks
期刊介绍: Protein Engineering, Design and Selection (PEDS) publishes high-quality research papers and review articles relevant to the engineering, design and selection of proteins for use in biotechnology and therapy, and for understanding the fundamental link between protein sequence, structure, dynamics, function, and evolution.
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