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Incorporation of Conformationally Constrained β ‐ Amino Acids into Peptides
Author(s) -
North Michael
Publication year - 2000
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/1099-1387(200007)6:7<301::aid-psc260>3.0.co;2-1
Subject(s) - desymmetrization , norbornene , antiparallel (mathematics) , chemistry , beta sheet , peptide , stereochemistry , amino acid , cyclopropane , beta (programming language) , trimer , enantioselective synthesis , organic chemistry , biochemistry , ring (chemistry) , catalysis , dimer , polymer , polymerization , physics , quantum mechanics , magnetic field , computer science , programming language
The use of norbornene units to induce the formation of β‐sheet and β‐turn type structures in peptides is discussed. The norbornene unit is readily prepared by a desymmetrization reaction and is easily incorporated into a peptide chain. Depending upon the exact nature of the norbornene unit, it is possible to form structures which resemble parallel β‐sheets, antiparallel β‐sheets or β‐turns. Similar peptide analogues incorporating a cis ‐2‐amino‐cyclopropane carboxylic acid unit can also be prepared. As an illustration of the application of this chemistry, a short, asymmetric synthesis of conformationally constrained metalloprotease inhibitors is presented. Copyright © 2000 European Peptide Society and John Wiley & Sons, Ltd.