Incorporation of artificial receptors into a protein/peptide surface: a strategy for on/off type of switching of semisynthetic enzymes.
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.
Hamachi
I
I
Department of Chemistry & Biochemistry, Graduate School of Engineering, Kyushu University, Fukuoka, 812-8581, Japan. itarutcm@mbox.nc.kyushu-u.ac.jp
Watanabe
J I
JI
Eboshi
R
R
Hiraoka
T
T
Shinkai
S
S
D000595:Amino Acid Sequence; D001665:Binding Sites; D004795:Enzyme Stability; D007700:Kinetics; D008024:Ligands; D008027:Light; D008670:Metals / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009211:Myoglobin / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D015202:Protein Engineering; D011506:Proteins / Q000138:chemical synthesis / Q000737:chemistry*; D012260:Ribonucleases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D008024:Ligands; D008670:Metals; D009211:Myoglobin; D011506:Proteins; D012260:Ribonucleases; C022542:ribonuclease S