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Peptides containing the sulfonamide junction: Synthesis, structure, and conformation of Z‐Tau‐Pro‐Phe‐NHiPr
Author(s) -
Calcagni A.,
Rossi D.,
Paradisi M. Paglialunga,
Lucente G.,
Luisi G.,
Gavuzzo E.,
Mazza F.,
Pochetti G.,
Paci M.
Publication year - 1997
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(19970415)41:5<555::aid-bip7>3.0.co;2-l
Subject(s) - chemistry , tripeptide , intramolecular force , turn (biochemistry) , sulfonamide , stereochemistry , folding (dsp implementation) , derivative (finance) , crystal structure , peptide bond , dipeptide , crystallography , peptide , biochemistry , financial economics , electrical engineering , economics , engineering
The taurine (Tau) containing tripeptide derivative Z‐Tau‐Pro‐Phe‐NHiPr (1) has been synthesized as suitable sulfonamido‐pseudopeptide model to investigate formation and conformational properties of folded secondary structures stabilized by intramolecular H bonds directly involving the sulfonamide junction. In the crystal the pseudopeptide 1 adopts a type I β‐turn with the Pro and Phe residues located at the (i + 1) and (i + 2) corner positions, respectively. The turn is stabilized by a 4 → 1 H bond engaging one of the SO 2 oxygen atoms and the isopropylamide NH. In CDCl 3 solution the β‐turn folding is accompanied by a γ‐turn centered at the Pro and involving a 3 → 1 H bond between the SO 2 and the Phe NH. A comparison of the structural and conformational properties found in 1 with those of the already known sulfonamido‐pseudopeptides, with particular reference to the models containing the Tau‐Pro junction, is also reported. © 1997 John Wiley & Sons, Inc. Biopoly 41: 555–567, 1997.