Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine

Structural studies of pentapeptides containing an achiral block, built from two dehydroamino acid residues (ΔZPhe and ΔAla) and two glycines, as well as one chiral L-Val residue were performed using NMR spectroscopy. The key role of the L-Val residue in the generation of the secondary structure of p...

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Main Authors:	Michał Jewgiński, Joanna Krzciuk-Gula, Maciej Makowski, Rafał Latajka, Paweł Kafarski
Format:	Article
Language:	English
Published:	Beilstein-Institut 2014-03-01
Series:	Beilstein Journal of Organic Chemistry
Subjects:	conformation dehydroalanine dehydropeptide dehydrophenylalanine NMR
Online Access:	https://doi.org/10.3762/bjoc.10.58

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spelling	doaj-3a91b5dfb0404ae1a0dcea34d4ec85dc2021-02-02T07:50:14ZengBeilstein-InstitutBeilstein Journal of Organic Chemistry1860-53972014-03-0110166066610.3762/bjoc.10.581860-5397-10-58Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valineMichał Jewgiński0Joanna Krzciuk-Gula1Maciej Makowski2Rafał Latajka3Paweł Kafarski4Department of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, PolandDepartment of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, PolandFaculty of Chemistry, University of Opole, Oleska 48, 45-052 Opole, PolandDepartment of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, PolandDepartment of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, PolandStructural studies of pentapeptides containing an achiral block, built from two dehydroamino acid residues (ΔZPhe and ΔAla) and two glycines, as well as one chiral L-Val residue were performed using NMR spectroscopy. The key role of the L-Val residue in the generation of the secondary structure of peptides is discussed. The obtained results suggest that the strongest influence on the conformation of peptides arises from a valine residue inserted at the C-terminal position. The most ordered conformation was found for peptide Boc-Gly-ΔAla-Gly-ΔZPhe-Val-OMe (3), which adopts a right-handed helical conformation.https://doi.org/10.3762/bjoc.10.58conformationdehydroalaninedehydropeptidedehydrophenylalanineNMR
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Michał Jewgiński Joanna Krzciuk-Gula Maciej Makowski Rafał Latajka Paweł Kafarski
spellingShingle	Michał Jewgiński Joanna Krzciuk-Gula Maciej Makowski Rafał Latajka Paweł Kafarski Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine Beilstein Journal of Organic Chemistry conformation dehydroalanine dehydropeptide dehydrophenylalanine NMR
author_facet	Michał Jewgiński Joanna Krzciuk-Gula Maciej Makowski Rafał Latajka Paweł Kafarski
author_sort	Michał Jewgiński
title	Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine
title_short	Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine
title_full	Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine
title_fullStr	Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine
title_full_unstemmed	Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine
title_sort	conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of l-valine
publisher	Beilstein-Institut
series	Beilstein Journal of Organic Chemistry
issn	1860-5397
publishDate	2014-03-01
description	Structural studies of pentapeptides containing an achiral block, built from two dehydroamino acid residues (ΔZPhe and ΔAla) and two glycines, as well as one chiral L-Val residue were performed using NMR spectroscopy. The key role of the L-Val residue in the generation of the secondary structure of peptides is discussed. The obtained results suggest that the strongest influence on the conformation of peptides arises from a valine residue inserted at the C-terminal position. The most ordered conformation was found for peptide Boc-Gly-ΔAla-Gly-ΔZPhe-Val-OMe (3), which adopts a right-handed helical conformation.
topic	conformation dehydroalanine dehydropeptide dehydrophenylalanine NMR
url	https://doi.org/10.3762/bjoc.10.58
work_keys_str_mv	AT michałjewginski conformationofdehydropentapeptidescontainingfourachiralaminoacidresiduescontrollingtheroleoflvaline AT joannakrzciukgula conformationofdehydropentapeptidescontainingfourachiralaminoacidresiduescontrollingtheroleoflvaline AT maciejmakowski conformationofdehydropentapeptidescontainingfourachiralaminoacidresiduescontrollingtheroleoflvaline AT rafałlatajka conformationofdehydropentapeptidescontainingfourachiralaminoacidresiduescontrollingtheroleoflvaline AT pawełkafarski conformationofdehydropentapeptidescontainingfourachiralaminoacidresiduescontrollingtheroleoflvaline
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Conformation of dehydropentapeptides containing four achiral amino acid residues – controlling the role of L-valine

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