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• W783708 abstract "We describe concepts and methods for generating a family of engineered target-binding proteins designed on the scaffold of the 10th human fibronectin type III domain (10Fn3), an extremely stable, single-domain protein with an immunoglobulin-like fold but lacking disulfide bonds. Large libraries of possible target-binding proteins can be constructed on the 10Fn3 scaffold by diversifying the sequence and length of its surface loops, which are structurally analogous to antibody complementarity-determining regions. Target-binding proteins with high affinity and specificity are selected from 10Fn3-based libraries using in vitro evolution technologies such as phage display, mRNA display, or yeast-surface display. 10Fn3-based target-binding proteins have binding properties comparable to those of antibodies, but they are smaller, simpler in architecture, and more user-friendly; as a consequence, these proteins are excellent building blocks for the construction of multidomain, multifunctional chains. The ease of engineering and robust properties of 10Fn3-based target-binding proteins have been validated by multiple independent academic and industrial groups. In addition to performing well as specific in vitro detection reagents and research tools, 10Fn3-based binding proteins are being developed as therapeutics, with the most advanced candidate currently in Phase II clinical trials." @default.
• W783708 created "2016-06-24" @default.
• W783708 creator A5002775376 @default.
• W783708 creator A5026366958 @default.
• W783708 creator A5071333092 @default.
• W783708 date "2012-01-01" @default.
• W783708 modified "2023-10-16" @default.
• W783708 title "Target-Binding Proteins Based on the 10th Human Fibronectin Type III Domain (10Fn3)" @default.
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• W783708 doi "https://doi.org/10.1016/b978-0-12-396962-0.00006-9" @default.
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