Influence of Side Chain Restriction and NH --- p Interaction on the b-Turn Folding Modes of Dipeptides Incorporating Phenylalanine Cyclohexane Derivatives

We have synthesized the model dipeptides Piv-L-Pro-c6Phe-NH(i)pr, incorporating each of the two cis cyclohexane analogues of phenylalanine: (S,S)- and (R,R)-1-amino-2-phenylcyclohexanecarboxylic acid. Their structural analysis has been carried out in solution by 1H NMR and FTIR absorption spectrosco...

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Autores: Jiménez, A.I. [0000-0001-8057-4861], Cativiela, C., Gómez-Catalán, J., Pérez, J.J., Aubry, A., París, M., Marraud, M.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2000
País:España
Institución:Universidad de La Rioja (UR)
Repositorio:RIUR. Repositorio Institucional de la Universidad de La Rioja
OAI Identifier:oai:portal.dialnet.es:doc/5bbc6937b750603269e8175b
Acceso en línea:https://investigacion.unirioja.es/documentos/5bbc6937b750603269e8175b
Access Level:acceso abierto
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spelling Influence of Side Chain Restriction and NH --- p Interaction on the b-Turn Folding Modes of Dipeptides Incorporating Phenylalanine Cyclohexane DerivativesJiménez, A.I. [0000-0001-8057-4861]Cativiela, C.Gómez-Catalán, J.Pérez, J.J.Aubry, A.París, M.Marraud, M.We have synthesized the model dipeptides Piv-L-Pro-c6Phe-NH(i)pr, incorporating each of the two cis cyclohexane analogues of phenylalanine: (S,S)- and (R,R)-1-amino-2-phenylcyclohexanecarboxylic acid. Their structural analysis has been carried out in solution by 1H NMR and FTIR absorption spectroscopy and in the solid state by X-ray diffraction. In weakly polar chlorinated solvents, the (S,S)c6Phe-containing dipeptide mainly accommodates a type I β-turn, whereas the (R,R) residue shows a greater propensity to βII-folding. This behavior does not differ significantly from that exhibited by the analogous dipeptides containing L- and D-Phe. However, the L-Pro-L-Phe sequence has been shown to undergo a βI-to-βII transition in the presence of a strong solvating medium, such as DMSO, or in the crystalline state. Interestingly, Piv-L-Pro-(S,S)c6PheNH(i)pr, incorporating its cyclohexane analogue with χ1 fixed at +60°, retains the βI-folded structure under these conditions. Theoretical calculations, supported by the experimental data, indicate that a c6Phe-NH to aromatic π-orbitals interaction has an important influence on the observed β-folding preferences.2000info:eu-repo/semantics/articleSubtype: Articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://investigacion.unirioja.es/documentos/5bbc6937b750603269e8175breponame:RIUR. Repositorio Institucional de la Universidad de La Riojainstname:Universidad de La Rioja (UR)Inglésinfo:eu-repo/semantics/altIdentifier/doi/10.1021/JA993568Kinfo:eu-repo/semantics/altIdentifier/pissn/0002-7863Influence of Side Chain Restriction and NH --- p Interaction on the b-Turn Folding Modes of Dipeptides Incorporating Phenylalanine Cyclohexane Derivatives, 2000, vol. 122, núm. 24, pág. 5811-5821info:eu-repo/semantics/openAccessoai:portal.dialnet.es:doc/5bbc6937b750603269e8175b2026-06-14T12:47:17Z
dc.title.none.fl_str_mv Influence of Side Chain Restriction and NH --- p Interaction on the b-Turn Folding Modes of Dipeptides Incorporating Phenylalanine Cyclohexane Derivatives
title Influence of Side Chain Restriction and NH --- p Interaction on the b-Turn Folding Modes of Dipeptides Incorporating Phenylalanine Cyclohexane Derivatives
spellingShingle Influence of Side Chain Restriction and NH --- p Interaction on the b-Turn Folding Modes of Dipeptides Incorporating Phenylalanine Cyclohexane Derivatives
Jiménez, A.I. [0000-0001-8057-4861]
title_short Influence of Side Chain Restriction and NH --- p Interaction on the b-Turn Folding Modes of Dipeptides Incorporating Phenylalanine Cyclohexane Derivatives
title_full Influence of Side Chain Restriction and NH --- p Interaction on the b-Turn Folding Modes of Dipeptides Incorporating Phenylalanine Cyclohexane Derivatives
title_fullStr Influence of Side Chain Restriction and NH --- p Interaction on the b-Turn Folding Modes of Dipeptides Incorporating Phenylalanine Cyclohexane Derivatives
title_full_unstemmed Influence of Side Chain Restriction and NH --- p Interaction on the b-Turn Folding Modes of Dipeptides Incorporating Phenylalanine Cyclohexane Derivatives
title_sort Influence of Side Chain Restriction and NH --- p Interaction on the b-Turn Folding Modes of Dipeptides Incorporating Phenylalanine Cyclohexane Derivatives
dc.creator.none.fl_str_mv Jiménez, A.I. [0000-0001-8057-4861]
Cativiela, C.
Gómez-Catalán, J.
Pérez, J.J.
Aubry, A.
París, M.
Marraud, M.
author Jiménez, A.I. [0000-0001-8057-4861]
author_facet Jiménez, A.I. [0000-0001-8057-4861]
Cativiela, C.
Gómez-Catalán, J.
Pérez, J.J.
Aubry, A.
París, M.
Marraud, M.
author_role author
author2 Cativiela, C.
Gómez-Catalán, J.
Pérez, J.J.
Aubry, A.
París, M.
Marraud, M.
author2_role author
author
author
author
author
author
description We have synthesized the model dipeptides Piv-L-Pro-c6Phe-NH(i)pr, incorporating each of the two cis cyclohexane analogues of phenylalanine: (S,S)- and (R,R)-1-amino-2-phenylcyclohexanecarboxylic acid. Their structural analysis has been carried out in solution by 1H NMR and FTIR absorption spectroscopy and in the solid state by X-ray diffraction. In weakly polar chlorinated solvents, the (S,S)c6Phe-containing dipeptide mainly accommodates a type I β-turn, whereas the (R,R) residue shows a greater propensity to βII-folding. This behavior does not differ significantly from that exhibited by the analogous dipeptides containing L- and D-Phe. However, the L-Pro-L-Phe sequence has been shown to undergo a βI-to-βII transition in the presence of a strong solvating medium, such as DMSO, or in the crystalline state. Interestingly, Piv-L-Pro-(S,S)c6PheNH(i)pr, incorporating its cyclohexane analogue with χ1 fixed at +60°, retains the βI-folded structure under these conditions. Theoretical calculations, supported by the experimental data, indicate that a c6Phe-NH to aromatic π-orbitals interaction has an important influence on the observed β-folding preferences.
publishDate 2000
dc.date.none.fl_str_mv 2000
dc.type.none.fl_str_mv info:eu-repo/semantics/article
Subtype: Article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://investigacion.unirioja.es/documentos/5bbc6937b750603269e8175b
url https://investigacion.unirioja.es/documentos/5bbc6937b750603269e8175b
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1021/JA993568K
info:eu-repo/semantics/altIdentifier/pissn/0002-7863
Influence of Side Chain Restriction and NH --- p Interaction on the b-Turn Folding Modes of Dipeptides Incorporating Phenylalanine Cyclohexane Derivatives, 2000, vol. 122, núm. 24, pág. 5811-5821
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:RIUR. Repositorio Institucional de la Universidad de La Rioja
instname:Universidad de La Rioja (UR)
instname_str Universidad de La Rioja (UR)
reponame_str RIUR. Repositorio Institucional de la Universidad de La Rioja
collection RIUR. Repositorio Institucional de la Universidad de La Rioja
repository.name.fl_str_mv
repository.mail.fl_str_mv
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