Plant chimeric binding polypeptides for universal molecular recognition

Abstract

Libraries of nucleic acids encoding chimeric binding polypeptides based on plant scaffold polypeptide sequences. Also described are methods for generating the libraries.

Description

Background of the invention [0001] The binding specificity and affinity of a protein to a target is mainly determined by the amino acid sequence of the protein in one or more binding domains. Thus, altering the amino acid sequence of the relevant region reconfigures the binding properties of the protein. [0002] In nature, combinatorial changes in protein binding are best illustrated by the vast array of immunoglobulins produced by the immune system. Each immunoglobulin contains a set of short, virtually unique amino acid sequences called hypervariable regions (ie, protein-binding domains), and another set of longer, invariant sequences called constant regions. Despite the vast sequence diversity among the hypervariable regions in the immunoglobulin population, the constant regions form beta sheets that stabilize the three-dimensional structure of the protein. Each set of hypervariable regions confers binding specificity and affinity. Two heavy and two light chain immunogl...

AI Technical Summary

Problems solved by technology

Finally, the expression of mammalian proteins such as immunoglobulins (e.g. so-called "plant antibodies") in edible plants also raises potential issues of consumer acceptance and is therefore an obstacle to commercialization

This may effectively prevent the use of plant antibodies for many input and output traits in transgenic plants

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