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• W2084336971 abstract "Peptides within the knottin family have been shown to possess inherent stability, making them attractive scaffolds for the development of therapeutic and diagnostic agents. Given its remarkable stability to proteases, the cyclic peptide kalata B1 was employed as a scaffold to create a large knottin library displayed on the surface of E. coli. A library exceeding 109 variants was constructed by randomizing seven amino acids within a loop of the kalata B1 scaffold and screened using fluorescence-activated cell sorting to identify peptide ligands specific for the active site of human thrombin. Refolded thrombin binders exhibited high nanomolar affinities in solution and slow dissociation rates and were able to inhibit thrombin’s enzymatic activity. Importantly, 80% of a knottin-based thrombin inhibitor remained intact after a 2 h incubation both with trypsin and with chymotrypsin, demonstrating that modifying the kalata B1 sequence did not compromise its stability properties. In addition, the knottin variant mediated 20-fold enhanced affinity for thrombin, when compared to the same seven residue binding epitope constrained by a single disulfide bond. Our results indicate that peptide libraries derived from the kalata B1 scaffold can yield high-affinity protein ligands that retain the remarkable protease resistance associated with the parent scaffold. More generally, this strategy may prove useful in the development of stable peptide ligands suitable for in vivo applications." @default.
• W2084336971 created "2016-06-24" @default.
• W2084336971 creator A5021477625 @default.
• W2084336971 creator A5051485374 @default.
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• W2084336971 date "2011-06-16" @default.
• W2084336971 modified "2023-10-11" @default.
• W2084336971 title "Protease-Resistant Peptide Ligands from a Knottin Scaffold Library" @default.
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• W2084336971 doi "https://doi.org/10.1021/cb200039s" @default.
• W2084336971 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3158827" @default.
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