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• W2895074301 abstract "The rigid conformation of constrained bicyclic peptides provides a number of advantages over larger protein-based ligands, including better chemical stability, enhanced tissue penetration, and a wider field of possible applications. Selective chemical modification strategies are able to extend the scope of applications not only in a therapeutic manner but also for the development of novel tools for protein capturing, bioimaging, and targeted drug delivery. Herein, we report the synthesis of an adamantane-based, symmetrical, tetravalent, sulfhydryl-specific peptide linker. We have developed an in vitro two-step modification strategy that allows the generation of differently functionalized bicyclic peptides. This “tool kit” strategy was applied to cyclize and functionalize a phage-encoded peptide library bearing the sequence CX6CX6C. After phage display against a model target, isolated peptides show strong consensus sequences, indicating target-specific binding. The newly developed symmetric tetravalent linker opens new avenues for the combinatorial selection and functionalization of bicyclic peptide ligands with affinity to virtually any target." @default.
• W2895074301 created "2018-10-12" @default.
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• W2895074301 date "2018-10-01" @default.
• W2895074301 modified "2023-09-27" @default.
• W2895074301 title "The Symmetric Tetravalent Sulfhydryl-Specific Linker NATBA Facilitates a Combinatorial “Tool Kit” Strategy for Phage Display-Based Selection of Functionalized Bicyclic Peptides" @default.
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• W2895074301 doi "https://doi.org/10.1021/acsomega.8b01814" @default.
• W2895074301 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6217522" @default.
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