Conformation of a terminally protected βγ hybrid dipeptide Boc-Ant-Gpn-OMe stabilized by C6/C7hydrogen bonds-Reference-Cited by-同舟云学术

Conformation of a terminally protected βγ hybrid dipeptide Boc-Ant-Gpn-OMe stabilized by C6/C7hydrogen bonds

Published:2013-12-14 Issue:1 Volume:70 Page:46-49
ISSN:2053-2296
Container-title:Acta Crystallographica Section C Structural Chemistry
language:
Short-container-title:Acta Crystallogr C

Author:

Wani Naiem Ahmad,Gupta Vivek Kumar,Kant Rajni,Aravinda Subrayashastry,Rai Rajkishor

Abstract

The hybrid βγ dipeptide, methyl 2-[1-({2-[(tert-butoxycarbonyl)amino]benzamido}methyl)cyclohexyl]acetate (Boc-Ant-Gpn-OMe), C22H32N2O5, adopts a folded conformation stabilized by intramolecular six- (C6) and seven-membered (C7) hydrogen-bonded rings, together with weak C—H...O and C—H...π interactions, resulting in a ribbon-like structure.

Publisher

International Union of Crystallography (IUCr)

Subject

Materials Chemistry,Inorganic Chemistry,Physical and Theoretical Chemistry,Condensed Matter Physics

Link

http://journals.iucr.org/c/issues/2014/01/00/ov3042/ov3042.pdf

Reference36 articles.

1. Preparation of Achiral and of Enantiopure Geminally Disubstituted β-Amino Acids for β-Peptide Synthesis

2. β-Peptide Foldamers: Robust Helix Formation in a New Family of β-Amino Acid Oligomers

3. Residue-based control of helix shape in β-peptide oligomers

4. Synthesis and Structural Characterization of Helix-Forming β-Peptides: trans-2-Aminocyclopentanecarboxylic Acid Oligomers

5. Hybrid polypeptides: Gabapentin as a stereochemically constrained γ-amino acid residue

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