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. 2002 Aug;9(8):933-42.
doi: 10.1016/s1074-5521(02)00187-4.

Directed evolution of high-affinity antibody mimics using mRNA display

Lihui Xu  1 , Patti Aha, Ke Gu, Robert G Kuimelis, Markus Kurz, Terence Lam, Ai Ching Lim, Hongxiang Liu, Peter A Lohse, Lin Sun, Shawn Weng, Richard W Wagner, Dasa Lipovsek
Affiliations

Directed evolution of high-affinity antibody mimics using mRNA display

Lihui Xu et al. Chem Biol. 2002 Aug.

Abstract

We constructed a library of >10(12) unique, covalently coupled mRNA-protein molecules by randomizing three exposed loops of an immunoglobulin-like protein, the tenth fibronectin type III domain (10Fn3). The antibody mimics that bound TNF-alpha were isolated from the library using mRNA display. Ten rounds of selection produced 10Fn3 variants that bound TNF-alpha with dissociation constants (K(d)) between 1 and 24 nM. After affinity maturation, the lowest K(d) measured was 20 pM. Selected antibody mimics were shown to capture TNF-alpha when immobilized in a protein microarray. 10Fn3-based scaffold libraries and mRNA-display allow the isolation of high-affinity, specific antigen binding proteins; potential applications of such binding proteins include diagnostic protein microarrays and protein therapeutics.

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