噬菌体展示
噬菌体
肽库
计算生物学
突变体
肽
限制
融合蛋白
生物
氨基酸
噬菌体
选择(遗传算法)
分子生物学
肽序列
遗传学
计算机科学
大肠杆菌
生物化学
基因
人工智能
重组DNA
工程类
机械工程
作者
Alex Chang,Joey Ting,Alfonso Espada,Howard B. Broughton,Manuel Molina‐Martín,Sepideh Afshar
标识
DOI:10.1093/protein/gzaa023
摘要
Abstract 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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