Genetically modified proteins: functional improvement and chimeragenesis

Bioengineered. 2015;6(5):262-74. doi: 10.1080/21655979.2015.1075674. Epub 2015 Jul 25.

Abstract

This review focuses on the emerging role of site-specific mutagenesis and chimeragenesis for the functional improvement of proteins in areas where traditional protein engineering methods have been extensively used and practically exhausted. The novel path for the creation of the novel proteins has been created on the farther development of the new structure and sequence optimization algorithms for generating and designing the accurate structure models in result of x-ray crystallography studies of a lot of proteins and their mutant forms. Artificial genetic modifications aim to expand nature's repertoire of biomolecules. One of the most exciting potential results of mutagenesis or chimeragenesis finding could be design of effective diagnostics, bio-therapeutics and biocatalysts. A sampling of recent examples is listed below for the in vivo and in vitro genetically improvement of various binding protein and enzyme functions, with references for more in-depth study provided for the reader's benefit.

Keywords: activity; antibodies; enzymes; epitopes; hybrid proteins; lectins; molecular structure; site-specific mutagenesis; specificity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution / genetics*
  • Directed Molecular Evolution / methods*
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed / methods*
  • Protein Engineering / methods
  • Recombinant Proteins / chemistry*
  • Recombinant Proteins / genetics*
  • Recombinant Proteins / metabolism
  • Recombination, Genetic / genetics
  • Structure-Activity Relationship

Substances

  • Recombinant Proteins