To facilitate the preparation of beta-peptide libraries in parallel, we have adapted reaction conditions for the solid-phase synthesis of 14-helical beta-peptides for use in a multimode microwave reactor. The low temperature/pressure requirements of microwave-assisted beta-peptide synthesis were found to be compatible with multiwell filter plates composed of polypropylene. Microwave heating of the 96-well plate was sufficiently homogeneous to allow the rapid preparation of a beta-peptide library in acceptable purity.
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http://dx.doi.org/10.1021/cc0501099 | DOI Listing |
Chempluschem
April 2021
Department of Chemistry, Chungbuk National University, Cheongju, Chungbuk, 28644, Republic of Korea.
The conformational preferences of oligomers of δ-amino acid (δAc a) with a cyclopentyl constraint in the C -C bond of the backbone were investigated by using DFT methods in the gas phase and in solution. The folded structures with C H-bonded pseudocycles were most preferred for dimer and tetramer of δAc a residues both in chloroform and water. However, for the hexameric Ac-(δAc a) -NHMe, the mixed H helical structure was found to be most preferred in chloroform (populated at 68 %), whereas the H helical structure was the most dominant conformation in water (populated at 60 %).
View Article and Find Full Text PDFCell Chem Biol
February 2019
Department of Chemical and Biological Engineering, University of Wisconsin - Madison, Madison, WI 53706, USA. Electronic address:
Synthetic peptidomimetics of antimicrobial peptides (AMPs) are promising antimicrobial drug candidates because they promote membrane disruption and exhibit greater structural and proteolytic stability than natural AMPs. We previously reported selective antifungal 14-helical β-peptides, but the mechanism of antifungal toxicity of β-peptides remains unknown. To provide insight into the mechanism, we studied antifungal β-peptide binding to artificial membranes and living Candida albicans cells.
View Article and Find Full Text PDFChemistry
February 2019
Institut für Organische und Biomolekulare Chemie, Georg-August-Universität Göttingen, Tammannstrasse 2, 37077, Göttingen, Germany.
β-Peptides are an interesting new class of transmembrane model peptides based on their conformationally stable and well-defined secondary structures. Herein, we present the synthesis of the paramagnetic β-amino acid β -hTOPP (4-(3,3,5,5-tetramethyl-2,6-dioxo-4-oxylpiperazin-1-yl)-d-β -homophenylglycine) that enables investigations of β-peptides by EPR spectroscopy. This amino acid adds to the, to date, sparse number of β-peptide spin labels.
View Article and Find Full Text PDFBiopolymers
January 2017
Molecular Biophysics Unit, Indian Institute of Science, Bangalore, 560 012, India.
Novel helical, structures unprecedented in the chemistry of α-polypeptides, may be found in polypeptides containing β and γ amino acids. The structural characterization of C and C -helices in oligo β-peptides was originally achieved using conformationally constrained cyclic β-residues. This study explores the conformational characteristics of proteinogenic β residues in homooligomeric sequences and addresses the issue of inducing a transition between C and C helices by the introduction of a guest α-residue.
View Article and Find Full Text PDFOrg Biomol Chem
January 2016
Department of Chemistry, Garware Research Centre, Savitribai Phule Pune University (Formerly University of Pune), Pune - 411 007, India.
Correction for 'Multivalent presentation of carbohydrates by 314-helical peptide templates: synthesis, conformational analysis using CD spectroscopy and saccharide recognition' by Nitin J. Pawar et al., Org.
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