Design of artificial supramolecular protein assemblies by enzymatic bioconjugation for biocatalytic reactions

Geisa A.L.G. Budinova, Yutaro Mori, Noriho Kamiya

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Self-assembly processes in biological systems generate well-organized, higherorder protein structures with unique functions. This chapter focuses on enzymatic strategies for assembling functional proteins by site-specific conjugation and site-specific ligand-receptor interaction. It discusses the potential of peptide tag-specific, enzymatic conjugation techniques by transglutaminase and horseradish peroxidase (HRP) to design biocatalytic assemblies with different modalities, including the use of different materials. The assembly of functional proteins in biological systems occurs by the natural affinity of two or more proteins in vivo. There are several forms of supramolecular protein assemblies in nature, which support the creation of artificial biomolecular systems. The use of self-assembled peptide systems, by non-covalent interactions, to design novel functional fibers and nanomaterial has several advantages over chemical systems, such as biocompatibility, easy synthesis, low toxicity, and functionaliz-ability. The non-covalent, strong, and specific molecular interaction between streptavidin and biotin is widely reported and has been applied in different areas.

Original languageEnglish
Title of host publicationEmerging Areas in Bioengineering
Publisherwiley
Pages93-103
Number of pages11
ISBN (Electronic)9783527803286
ISBN (Print)9783527340880
DOIs
Publication statusPublished - Jan 1 2017

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

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