Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Peptides containing the sulfonamide junction. 2. Structure and conformation of Z–Tau–Pro– D ‐Phe–NHiPr

Peptides containing the sulfonamide junction. 2. Structure and conformation of Z–Tau–Pro– D... The taurine (Tau) containing N‐protected pseudotripeptide isopropylamide Z–Tau–Pro–D‐Phe–NHiPr (1) has been specifically designed and synthesized as suitable model to test the ability of the sulfonamido group to participate as H‐bond acceptor to a type II β‐turn and to get information on the preferred rotameric conformation around the S—N bond and the hybridization state of the nitrogen atom. The present structural investigation reveals that, although the sulfonamide junction is invariably folded in a gauche mode, the β‐turn structure, stabilized by the 4 → 1 hydrogen bond, is not found in the crystal and the sulfonamido oxygen atoms are not involved in any intra‐ or intermolecular hydrogen‐bond interaction. More than one conformer populates the CDCl3 solution with only a minor contribution by the expected β‐turn. The Pro nitrogen is significantly pyramidalized and the nitrogen lone pair points in opposite direction to that of the Pro CαH bond thus adopting R chirality, in an arrangement practically identical to that found in the previously studied homochiral analogue Z–Tau–Pro–Phe–NHiPr. © 2000 John Wiley & Sons, Inc. Biopoly 54: 379–387, 2000 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biopolymers Wiley

Peptides containing the sulfonamide junction. 2. Structure and conformation of Z–Tau–Pro– D ‐Phe–NHiPr

Download PDF
9 pages

Loading next page...
 
/lp/wiley/peptides-containing-the-sulfonamide-junction-2-structure-and-zTsx0F8UNl

References (0)

References for this paper are not available at this time. We will be adding them shortly, thank you for your patience.

Publisher
Wiley
Copyright
Copyright © 2000 John Wiley & Sons, Inc.
ISSN
0006-3525
eISSN
1097-0282
DOI
10.1002/1097-0282(200011)54:6<379::AID-BIP20>3.3.CO;2-E
Publisher site
See Article on Publisher Site

Abstract

The taurine (Tau) containing N‐protected pseudotripeptide isopropylamide Z–Tau–Pro–D‐Phe–NHiPr (1) has been specifically designed and synthesized as suitable model to test the ability of the sulfonamido group to participate as H‐bond acceptor to a type II β‐turn and to get information on the preferred rotameric conformation around the S—N bond and the hybridization state of the nitrogen atom. The present structural investigation reveals that, although the sulfonamide junction is invariably folded in a gauche mode, the β‐turn structure, stabilized by the 4 → 1 hydrogen bond, is not found in the crystal and the sulfonamido oxygen atoms are not involved in any intra‐ or intermolecular hydrogen‐bond interaction. More than one conformer populates the CDCl3 solution with only a minor contribution by the expected β‐turn. The Pro nitrogen is significantly pyramidalized and the nitrogen lone pair points in opposite direction to that of the Pro CαH bond thus adopting R chirality, in an arrangement practically identical to that found in the previously studied homochiral analogue Z–Tau–Pro–Phe–NHiPr. © 2000 John Wiley & Sons, Inc. Biopoly 54: 379–387, 2000

Journal

Biopolymers – Wiley

Published: Nov 1, 2000

Keywords: conformation; crystal structure; nitrogen pyramidalization; pseudopeptides; sulfonamides; sulfonamido‐peptides; taurine

There are no references for this article.