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Parametrization of synthetic amino acids

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Resumo:C(alpha)-C(alpha)dialkylglycines, sarcosine, O-methyltyrosine and beta-(imidazol-1-yl)-alanine are noncoded amino acids with a large pharmaceutical potential. We have developed a set of parameters for these amino acids, consistent with the AMBER force field. Several dipeptide and tripeptide models were built to simulate the different possibilities for insertion of the noncoded amino acids in a peptide backbone. Bonding parameters were obtained from both existing force fields and quantum calculations. The Coulombic parameters have been determined using a multiconformational weighted approach and a restricted electrostatic potential fitting, at a 6-31G* ab initio level. Molecular dynamics simulations have been carried out on the model peptides to validate the parameters obtained. The characteristic geometry features such as the planarity of peptide bonds have been conserved on these models. The peptide models, which included monosubstituted residues, have revealed considerable backbone flexibility. The conformational flexibility of the peptides containing disubstituted residues has been significantly restricted by the length and volume of their side chains.
Autores principais:Preto, Marco A. C.
Outros Autores:Melo, André; Costa, Susana P. G.; Maia, Hernâni Lopes Silva; Ramos, Maria J.
Assunto:Ciências Naturais::Ciências Químicas
Ano:2003
País:Portugal
Tipo de documento:artigo
Tipo de acesso:acesso restrito
Instituição associada:Universidade do Minho
Idioma:inglês
Origem:RepositóriUM - Universidade do Minho
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author Preto, Marco A. C.
author2 Melo, André
Costa, Susana P. G.
Maia, Hernâni Lopes Silva
Ramos, Maria J.
author2_role author
author
author
author
author_facet Preto, Marco A. C.
Melo, André
Costa, Susana P. G.
Maia, Hernâni Lopes Silva
Ramos, Maria J.
author_role author
contributor_name_str_mv RepositóriUM - Universidade do Minho
country_str PT
creators_json_txt [{\"Person.name\":\"Preto, Marco A. C.\"},{\"Person.name\":\"Melo, André\"},{\"Person.name\":\"Costa, Susana P. G.\"},{\"Person.name\":\"Maia, Hernâni Lopes Silva\"},{\"Person.name\":\"Ramos, Maria J.\"}]
datacite.contributors.contributor.contributorName.fl_str_mv RepositóriUM - Universidade do Minho
datacite.creators.creator.creatorName.fl_str_mv Preto, Marco A. C.
Melo, André
Costa, Susana P. G.
Maia, Hernâni Lopes Silva
Ramos, Maria J.
datacite.date.Accepted.fl_str_mv 2003-01-01T00:00:00Z
datacite.date.embargoed.fl_str_mv 10000-01-01T00:00:00Z
datacite.rights.fl_str_mv http://purl.org/coar/access_right/c_16ec
datacite.subjects.subject.fl_str_mv Ciências Naturais::Ciências Químicas
datacite.titles.title.fl_str_mv Parametrization of synthetic amino acids
dc.contributor.none.fl_str_mv RepositóriUM - Universidade do Minho
dc.creator.none.fl_str_mv Preto, Marco A. C.
Melo, André
Costa, Susana P. G.
Maia, Hernâni Lopes Silva
Ramos, Maria J.
dc.date.Accepted.fl_str_mv 2003-01-01T00:00:00Z
dc.date.embargoed.fl_str_mv 10000-01-01T00:00:00Z
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.identifier.none.fl_str_mv https://hdl.handle.net/1822/86454
dc.language.none.fl_str_mv eng
dc.publisher.none.fl_str_mv American Chemical Society
dc.rights.none.fl_str_mv http://purl.org/coar/access_right/c_16ec
dc.subject.none.fl_str_mv Ciências Naturais::Ciências Químicas
dc.title.fl_str_mv Parametrization of synthetic amino acids
dc.type.none.fl_str_mv http://purl.org/coar/resource_type/c_6501
description C(alpha)-C(alpha)dialkylglycines, sarcosine, O-methyltyrosine and beta-(imidazol-1-yl)-alanine are noncoded amino acids with a large pharmaceutical potential. We have developed a set of parameters for these amino acids, consistent with the AMBER force field. Several dipeptide and tripeptide models were built to simulate the different possibilities for insertion of the noncoded amino acids in a peptide backbone. Bonding parameters were obtained from both existing force fields and quantum calculations. The Coulombic parameters have been determined using a multiconformational weighted approach and a restricted electrostatic potential fitting, at a 6-31G* ab initio level. Molecular dynamics simulations have been carried out on the model peptides to validate the parameters obtained. The characteristic geometry features such as the planarity of peptide bonds have been conserved on these models. The peptide models, which included monosubstituted residues, have revealed considerable backbone flexibility. The conformational flexibility of the peptides containing disubstituted residues has been significantly restricted by the length and volume of their side chains.
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instname_str Universidade do Minho
language eng
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oai_identifier_str oai:repositorium.uminho.pt:1822/86454
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person_str_mv Preto, Marco A. C.
Melo, André
Costa, Susana P. G.
Maia, Hernâni Lopes Silva
Ramos, Maria J.
publishDate 2003
publisher.none.fl_str_mv American Chemical Society
reponame_str RepositóriUM - Universidade do Minho
repository_id_str urn:repositoryAcronym:rum
service_str_mv urn:repositoryAcronym:rum
spelling engAmerican Chemical SocietyporC(alpha)-C(alpha)dialkylglycines, sarcosine, O-methyltyrosine and beta-(imidazol-1-yl)-alanine are noncoded amino acids with a large pharmaceutical potential. We have developed a set of parameters for these amino acids, consistent with the AMBER force field. Several dipeptide and tripeptide models were built to simulate the different possibilities for insertion of the noncoded amino acids in a peptide backbone. Bonding parameters were obtained from both existing force fields and quantum calculations. The Coulombic parameters have been determined using a multiconformational weighted approach and a restricted electrostatic potential fitting, at a 6-31G* ab initio level. Molecular dynamics simulations have been carried out on the model peptides to validate the parameters obtained. The characteristic geometry features such as the planarity of peptide bonds have been conserved on these models. The peptide models, which included monosubstituted residues, have revealed considerable backbone flexibility. The conformational flexibility of the peptides containing disubstituted residues has been significantly restricted by the length and volume of their side chains.application/pdfapplication/pdfporParametrization of synthetic amino acidsPreto, Marco A. C.Melo, AndréCosta, Susana P. G.Maia, Hernâni Lopes SilvaRamos, Maria J.HostingInstitutionOrganizationalRepositóriUM - Universidade do Minhoe-mailmailto:repositorium@usdb.uminho.ptrepositorium@usdb.uminho.ptCITATIONPreto, M. A. C., Melo, A., Costa, S. P. G., Maia, H. L. S., & Ramos, M. J. (2003, November 27). Parametrization of Synthetic Amino Acids. The Journal of Physical Chemistry B. American Chemical Society (ACS). http://doi.org/10.1021/jp030544yISSNIsPartOf1520-6106DOIIsPartOf10.1021/jp030544y20032023-08-20T15:52:47Z10000-01-01T00:00:00Z2003-01-01T00:00:00ZHandlehttps://hdl.handle.net/1822/86454http://purl.org/coar/access_right/c_16ecrestricted accesshttp://www.oecd.org/science/inno/38235147.pdfFields of Science and Technology (FOS)Ciências Naturais::Ciências Químicas288680 bytes391450 bytesliteraturehttp://purl.org/coar/resource_type/c_6501journal articlehttp://purl.org/coar/access_right/c_f1cfapplication/pdffulltexthttps://repositorium.uminho.pt/bitstreams/e4f4eef2-7a2e-4dd7-909f-eb5e06dddddf/downloadhttp://purl.org/coar/access_right/c_f1cfapplication/pdffulltexthttps://repositorium.uminho.pt/bitstreams/47609df9-e761-485a-920f-8e99b10621bc/download
spellingShingle Parametrization of synthetic amino acids
Preto, Marco A. C.
Ciências Naturais::Ciências Químicas
status SINGLETON
subject.other.fl_str_mv Ciências Naturais::Ciências Químicas
title Parametrization of synthetic amino acids
title_full Parametrization of synthetic amino acids
title_fullStr Parametrization of synthetic amino acids
title_full_unstemmed Parametrization of synthetic amino acids
title_short Parametrization of synthetic amino acids
title_sort Parametrization of synthetic amino acids
topic Ciências Naturais::Ciências Químicas
topic_facet Ciências Naturais::Ciências Químicas
url https://hdl.handle.net/1822/86454
visible 1