14-Helical folding in a cyclobutane-containing β-tetrapeptide

Autores
Izquierdo, Sandra; Kogan, Marcelo Javier; Parella, Teodor; Moglioni, Albertina Gladys; Branchadell, Vicenc; Giralt, Ernest; Ortuño, Rosa M.
Año de publicación
2004
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The efficient synthesis of tetrapeptide 5 containing, in alternation, cyclobutane and β-alanine residues is described. NMR experiments both at low temperature in CDCl3 and at 298 K in DMSO-d6 solutions show the contribution of a strong hydrogen bond in the folded major conformation of 5. Temperature coefficients and diffusion times point out a hydrogen bond involving the NH proton from the cyclobutane residue 1 whereas NOEs manifest the high rigidity of the central fragment of the molecule and are compatible with a 14-membered macrocycle. Theoretical calculations predict a most stable folded conformation corresponding to a 14-helix stabilized by a hydrogen bond between NH10 in the first residue and OC25 in the third residue. This structure remains unaltered during the molecular dynamics simulation at 298 K in chloroform. All these results provide evidence for a 14-helical folding and reveal the ability of cis-2-aminocyclobutane carboxylic acid residues to promote folded conformations when incorporated into β-peptides.
Fil: Izquierdo, Sandra. Universitat Autònoma de Barcelona; España
Fil: Kogan, Marcelo Javier. Institut de Recerca Biomédica; España
Fil: Parella, Teodor. Universitat Autònoma de Barcelona; España
Fil: Moglioni, Albertina Gladys. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Metabolismo del Fármaco. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Metabolismo del Fármaco; Argentina
Fil: Branchadell, Vicenc. Universitat Autònoma de Barcelona; España
Fil: Giralt, Ernest. Institut de Recerca Biomédica; España
Fil: Ortuño, Rosa M.. Universitat Autònoma de Barcelona; España
Materia
helical folding
peptides
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/137894
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/137894
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 14-Helical folding in a cyclobutane-containing β-tetrapeptideIzquierdo, SandraKogan, Marcelo JavierParella, TeodorMoglioni, Albertina GladysBranchadell, VicencGiralt, ErnestOrtuño, Rosa M.helical foldingpeptideshttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The efficient synthesis of tetrapeptide 5 containing, in alternation, cyclobutane and β-alanine residues is described. NMR experiments both at low temperature in CDCl3 and at 298 K in DMSO-d6 solutions show the contribution of a strong hydrogen bond in the folded major conformation of 5. Temperature coefficients and diffusion times point out a hydrogen bond involving the NH proton from the cyclobutane residue 1 whereas NOEs manifest the high rigidity of the central fragment of the molecule and are compatible with a 14-membered macrocycle. Theoretical calculations predict a most stable folded conformation corresponding to a 14-helix stabilized by a hydrogen bond between NH10 in the first residue and OC25 in the third residue. This structure remains unaltered during the molecular dynamics simulation at 298 K in chloroform. All these results provide evidence for a 14-helical folding and reveal the ability of cis-2-aminocyclobutane carboxylic acid residues to promote folded conformations when incorporated into β-peptides.Fil: Izquierdo, Sandra. Universitat Autònoma de Barcelona; EspañaFil: Kogan, Marcelo Javier. Institut de Recerca Biomédica; EspañaFil: Parella, Teodor. Universitat Autònoma de Barcelona; EspañaFil: Moglioni, Albertina Gladys. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Metabolismo del Fármaco. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Metabolismo del Fármaco; ArgentinaFil: Branchadell, Vicenc. Universitat Autònoma de Barcelona; EspañaFil: Giralt, Ernest. Institut de Recerca Biomédica; EspañaFil: Ortuño, Rosa M.. Universitat Autònoma de Barcelona; EspañaAmerican Chemical Society2004-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/137894Izquierdo, Sandra; Kogan, Marcelo Javier; Parella, Teodor; Moglioni, Albertina Gladys; Branchadell, Vicenc; et al.; 14-Helical folding in a cyclobutane-containing β-tetrapeptide; American Chemical Society; Journal of Organic Chemistry; 69; 15; 8-2004; 5093-50990022-3263CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/jo0497555info:eu-repo/semantics/altIdentifier/doi/10.1021/jo0497555info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:36:22Zoai:ri.conicet.gov.ar:11336/137894instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:36:22.387CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv 14-Helical folding in a cyclobutane-containing β-tetrapeptide
title 14-Helical folding in a cyclobutane-containing β-tetrapeptide
spellingShingle 14-Helical folding in a cyclobutane-containing β-tetrapeptide
Izquierdo, Sandra
helical folding
peptides
title_short 14-Helical folding in a cyclobutane-containing β-tetrapeptide
title_full 14-Helical folding in a cyclobutane-containing β-tetrapeptide
title_fullStr 14-Helical folding in a cyclobutane-containing β-tetrapeptide
title_full_unstemmed 14-Helical folding in a cyclobutane-containing β-tetrapeptide
title_sort 14-Helical folding in a cyclobutane-containing β-tetrapeptide
dc.creator.none.fl_str_mv Izquierdo, Sandra
Kogan, Marcelo Javier
Parella, Teodor
Moglioni, Albertina Gladys
Branchadell, Vicenc
Giralt, Ernest
Ortuño, Rosa M.
author Izquierdo, Sandra
author_facet Izquierdo, Sandra
Kogan, Marcelo Javier
Parella, Teodor
Moglioni, Albertina Gladys
Branchadell, Vicenc
Giralt, Ernest
Ortuño, Rosa M.
author_role author
author2 Kogan, Marcelo Javier
Parella, Teodor
Moglioni, Albertina Gladys
Branchadell, Vicenc
Giralt, Ernest
Ortuño, Rosa M.
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv helical folding
peptides
topic helical folding
peptides
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The efficient synthesis of tetrapeptide 5 containing, in alternation, cyclobutane and β-alanine residues is described. NMR experiments both at low temperature in CDCl3 and at 298 K in DMSO-d6 solutions show the contribution of a strong hydrogen bond in the folded major conformation of 5. Temperature coefficients and diffusion times point out a hydrogen bond involving the NH proton from the cyclobutane residue 1 whereas NOEs manifest the high rigidity of the central fragment of the molecule and are compatible with a 14-membered macrocycle. Theoretical calculations predict a most stable folded conformation corresponding to a 14-helix stabilized by a hydrogen bond between NH10 in the first residue and OC25 in the third residue. This structure remains unaltered during the molecular dynamics simulation at 298 K in chloroform. All these results provide evidence for a 14-helical folding and reveal the ability of cis-2-aminocyclobutane carboxylic acid residues to promote folded conformations when incorporated into β-peptides.
Fil: Izquierdo, Sandra. Universitat Autònoma de Barcelona; España
Fil: Kogan, Marcelo Javier. Institut de Recerca Biomédica; España
Fil: Parella, Teodor. Universitat Autònoma de Barcelona; España
Fil: Moglioni, Albertina Gladys. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Metabolismo del Fármaco. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Metabolismo del Fármaco; Argentina
Fil: Branchadell, Vicenc. Universitat Autònoma de Barcelona; España
Fil: Giralt, Ernest. Institut de Recerca Biomédica; España
Fil: Ortuño, Rosa M.. Universitat Autònoma de Barcelona; España
description The efficient synthesis of tetrapeptide 5 containing, in alternation, cyclobutane and β-alanine residues is described. NMR experiments both at low temperature in CDCl3 and at 298 K in DMSO-d6 solutions show the contribution of a strong hydrogen bond in the folded major conformation of 5. Temperature coefficients and diffusion times point out a hydrogen bond involving the NH proton from the cyclobutane residue 1 whereas NOEs manifest the high rigidity of the central fragment of the molecule and are compatible with a 14-membered macrocycle. Theoretical calculations predict a most stable folded conformation corresponding to a 14-helix stabilized by a hydrogen bond between NH10 in the first residue and OC25 in the third residue. This structure remains unaltered during the molecular dynamics simulation at 298 K in chloroform. All these results provide evidence for a 14-helical folding and reveal the ability of cis-2-aminocyclobutane carboxylic acid residues to promote folded conformations when incorporated into β-peptides.
publishDate 2004
dc.date.none.fl_str_mv 2004-08
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/137894
Izquierdo, Sandra; Kogan, Marcelo Javier; Parella, Teodor; Moglioni, Albertina Gladys; Branchadell, Vicenc; et al.; 14-Helical folding in a cyclobutane-containing β-tetrapeptide; American Chemical Society; Journal of Organic Chemistry; 69; 15; 8-2004; 5093-5099
0022-3263
CONICET Digital
CONICET
url http://hdl.handle.net/11336/137894
identifier_str_mv Izquierdo, Sandra; Kogan, Marcelo Javier; Parella, Teodor; Moglioni, Albertina Gladys; Branchadell, Vicenc; et al.; 14-Helical folding in a cyclobutane-containing β-tetrapeptide; American Chemical Society; Journal of Organic Chemistry; 69; 15; 8-2004; 5093-5099
0022-3263
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/jo0497555
info:eu-repo/semantics/altIdentifier/doi/10.1021/jo0497555
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1844613140139999232
score 13.070432

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