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Induced Axial Chirality in the Biphenyl Core of the Proatropoisomeric, C α ‐Tetrasubstituted α‐Amino Acid Residue Bip in Peptides
Author(s) -
Mazaleyrat JeanPaul,
Wright Karen,
Gaucher Anne,
Toulemonde Nathalie,
Dutot Laurence,
Wakselman Michel,
Broxterman Quirinus B.,
Kaptein Bernard,
Oancea Simona,
Peggion Cristina,
Crisma Marco,
Formaggio Fernando,
Toniolo Claudio
Publication year - 2005
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200500187
Subject(s) - dipeptide , residue (chemistry) , chirality (physics) , chemistry , stereochemistry , biphenyl , peptide , amino acid , axial chirality , amino acid residue , peptide sequence , chiral symmetry , catalysis , organic chemistry , enantioselective synthesis , biochemistry , physics , quantum mechanics , nambu–jona lasinio model , gene , quark
An induced axial chirality in the biphenyl core of the 2′,1′:1,2;1′′,2′′:3,4‐dibenzcyclohepta‐1,3‐diene‐6‐amino‐6‐carboxylic acid (Bip) residue, a conformationally labile, atropoisomeric, C α ‐tetrasubstituted α‐amino acid, was observed by CD and 1 H NMR spectroscopic techniques in the linear dipeptides Boc‐Bip‐Xaa*‐OMe where Boc= tert ‐butoxycarbonyl, OMe=methoxy, and Xaa*= D ‐ and/or L ‐ Ala, ‐Val, ‐Leu, ‐Phe, ‐(αMe)Val and ‐(αMe)Leu. Chiral induction was significantly lower in the isomeric dipeptides Boc‐Xaa*‐Bip‐OMe, with the Xaa* residue located at the N‐terminus of Bip, as well as in the cyclic dipeptide cyclo‐[Bip‐ L ‐ Ala]. The results obtained in solution were confirmed by X‐ray diffraction analysis of a crystalline sample of Boc‐( R )‐Bip‐ D ‐Ala‐OMe.
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