Incorporation of artificial receptors into a protein/peptide surface

A strategy for on/off type of switching of semisynthetic enzymes

Itaru Hamachi, Jun Ichi Watanabe, Ryoji Eboshi, Takashi Hiraoka, Seiji Shinkai

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Recent developments in new bioorganic methodologies have greatly facilitated the site-specific incorporation of non-natural amino acids into the protein framework. It is now desirable for chemists to explore promising concepts based on chemistry for regulation and extension of functions of naturally occurring enzymes using non-natural molecules, in order to promote the new trends in protein/enzyme engineering. This article demonstrates that the concepts of host - guest (or supramolecular) chemistry, which have been developed over the last few decades, provide powerful tools for the artificial control of the functions of native proteins and enzymes.

Original languageEnglish
Pages (from-to)459-468
Number of pages10
JournalBiopolymers - Peptide Science Section
Volume55
Issue number6
DOIs
Publication statusPublished - Dec 1 2000

Fingerprint

Artificial Receptors
Peptides
Membrane Proteins
Enzymes
Proteins
Supramolecular chemistry
Protein Engineering
Amino acids
Amino Acids
Molecules

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Biomaterials
  • Organic Chemistry

Cite this

Incorporation of artificial receptors into a protein/peptide surface : A strategy for on/off type of switching of semisynthetic enzymes. / Hamachi, Itaru; Watanabe, Jun Ichi; Eboshi, Ryoji; Hiraoka, Takashi; Shinkai, Seiji.

In: Biopolymers - Peptide Science Section, Vol. 55, No. 6, 01.12.2000, p. 459-468.

Research output: Contribution to journalArticle

Hamachi, Itaru ; Watanabe, Jun Ichi ; Eboshi, Ryoji ; Hiraoka, Takashi ; Shinkai, Seiji. / Incorporation of artificial receptors into a protein/peptide surface : A strategy for on/off type of switching of semisynthetic enzymes. In: Biopolymers - Peptide Science Section. 2000 ; Vol. 55, No. 6. pp. 459-468.
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