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Design, synthesis, and conformational analysis of azacycloalkane amino acids as conformationally constrained probes for mimicry of peptide secondary structures
Author(s) -
Halab Liliane,
Gosselin Francis,
Lubell William D.
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)55:2<101::aid-bip20>3.0.co;2-o
Subject(s) - dipeptide , chemistry , amino acid , peptide , mimicry , combinatorial chemistry , stereochemistry , peptide synthesis , biochemistry , ecology , biology
Conformationally constrained amino acid and dipeptide units can serve in mimics of specific secondary structures for studying relationships between peptide conformation and biological activity. A variety of mimics are required to study systematically the structure–activity relationships in biologically relevant peptides. We present our efforts on the design, synthesis, and conformational analysis of a series of rigid surrogates of amino acid and dipeptide units for application within constrained peptide analogues, and for employment as inputs for combinatorial science. Conceived to be general and versatile, our methodology has delivered a variety of azacycloalkane and azabicycloalkane amino acids in enantiomerically pure form, via practical methods, from readily available and inexpensive starting materials. ©2000 John Wiley & Sons, Inc. Biopoly 55: 101–122, 2000