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Artificial peptides with unnatural components designed for materializing protein function
Author(s) -
Ishida Hitoshi,
Inoue Yoshihisa
Publication year - 2000
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/1097-0282(2000)55:6<469::aid-bip1022>3.0.co;2-l
Subject(s) - chemistry , ruthenium , peptide , amino acid , hydrolysis , rational design , phenylalanine , stereochemistry , combinatorial chemistry , molecule , cyclic peptide , conjugate , catalysis , organic chemistry , biochemistry , nanotechnology , materials science , mathematical analysis , mathematics
In order to design functional peptides, we employed two strategies. The first one is to incorporate rigid unnatural amino acids into peptides to make the peptide backbone rigid. Functions were expected to appear through the conformational control by the strategy. A series of cyclic peptides constituted of alternating natural amino acids and 3‐aminobenzoic acid, used as an unnatural amino acid, were synthesized. These cyclic peptides were found to function as strong binders for phosphomonoester, catalysts for ester hydrolysis, and/or ion channels. The second strategy is to conjugate peptides with unnatural and inherently functional molecules. Following this strategy, oligo( L ‐leucine)‐ or oligo( L ‐phenylalanine)‐modified ruthenium tris(bipyridine) complexes were synthesized. Distance dependence of the photoinduced electron transfer from the ruthenium complexes and the function as sensors for phosphate anion (H 2 PO − 4 ) are discussed. © 2001 John Wiley & Sons, Inc. Biopolymers (Pept Sci) 55: 469–478, 2000