Peptide solubility, structure and charge position effect on adsorption by aluminium hydroxide

Solubility, structure and position of charges in a peptide antigen sequence can be mentioned as being amongst the basic features of adsorption. In order to study their effect on adsorption, seven analogue series were synthesized from a MSP-1 peptide sequence by systematically replacing each one of t...

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Autores:
Trujillo, Mary
Valencia, Jesus
Calvo, Julio
Tipo de recurso:
Article of journal
Fecha de publicación:
2006
Institución:
Universidad Nacional de Colombia
Repositorio:
Universidad Nacional de Colombia
Idioma:
spa
OAI Identifier:
oai:repositorio.unal.edu.co:unal/22326
Acceso en línea:
https://repositorio.unal.edu.co/handle/unal/22326
http://bdigital.unal.edu.co/13360/
Palabra clave:
Adsorption
aluminium hydroxide
peptide analogues
solubility and adsorption
structure and adsorption
charge position and adsorption
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openAccess
License
Atribución-NoComercial 4.0 Internacional
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spelling Atribución-NoComercial 4.0 InternacionalDerechos reservados - Universidad Nacional de Colombiahttp://creativecommons.org/licenses/by-nc/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Trujillo, Marycd7b4462-fd78-40fc-9652-da5b9b56eb88300Valencia, Jesuscd2baa35-da86-46bb-8481-fb0f9109ec62300Calvo, Julio079985a9-46d3-4f46-ae07-9ea4905ac6bf3002019-06-25T20:34:56Z2019-06-25T20:34:56Z2006https://repositorio.unal.edu.co/handle/unal/22326http://bdigital.unal.edu.co/13360/Solubility, structure and position of charges in a peptide antigen sequence can be mentioned as being amongst the basic features of adsorption. In order to study their effect on adsorption, seven analogue series were synthesized from a MSP-1 peptide sequence by systematically replacing each one of the positions in the peptide sequence by aspartic acid, glutamic acid, serine, alanine, asparagine, glutamine or lysine. Such modifications in analogue peptide sequences showed a non-regular tendency regarding solubility and adsorption data. Aspartic acid and Glutamic acid analogue series showed great improvements in adsorption, especially in peptides where Lysine in position 6 and Arginine in position 13 were replaced. Solubility of position 5 analogue was greater than the position 6 analogue in Aspartic acid series; however, the position 6 analogue showed best adsorption results whilst the Aspartic acid in position 5 analogue showed no adsorption in the same conditions. Nuclear Magnetic Resonance structural analysis revealed differences in the -helical structureextension between these analogues. The Aspartic acid in position 6, located in the polar side of the helix, may allow this analogueto fit better onto the adsorption regions suggesting that the local electrostatic charge is responsible for this behavior.application/pdfspaUniversidad Nacional de Colombiahttp://revistas.unal.edu.co/index.php/rcolquim/article/view/854Universidad Nacional de Colombia Revistas electrónicas UN Revista Colombiana de QuímicaRevista Colombiana de QuímicaRevista Colombiana de Química; Vol. 35, núm. 2 (2006); 135-146 0120-2804Trujillo, Mary and Valencia, Jesus and Calvo, Julio (2006) Peptide solubility, structure and charge position effect on adsorption by aluminium hydroxide. Revista Colombiana de Química; Vol. 35, núm. 2 (2006); 135-146 0120-2804 .Peptide solubility, structure and charge position effect on adsorption by aluminium hydroxideArtículo de revistainfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1http://purl.org/coar/version/c_970fb48d4fbd8a85Texthttp://purl.org/redcol/resource_type/ARTAdsorptionaluminium hydroxidepeptide analoguessolubility and adsorptionstructure and adsorptioncharge position and adsorptionORIGINAL854-5884-1-PB.pdfapplication/pdf699128https://repositorio.unal.edu.co/bitstream/unal/22326/1/854-5884-1-PB.pdf6e78ade701534b483636949c9420a912MD51THUMBNAIL854-5884-1-PB.pdf.jpg854-5884-1-PB.pdf.jpgGenerated Thumbnailimage/jpeg7035https://repositorio.unal.edu.co/bitstream/unal/22326/2/854-5884-1-PB.pdf.jpgd3c061696a1ce284bc81642074a23690MD52unal/22326oai:repositorio.unal.edu.co:unal/223262022-10-14 23:02:11.155Repositorio Institucional Universidad Nacional de Colombiarepositorio_nal@unal.edu.co
dc.title.spa.fl_str_mv Peptide solubility, structure and charge position effect on adsorption by aluminium hydroxide
title Peptide solubility, structure and charge position effect on adsorption by aluminium hydroxide
spellingShingle Peptide solubility, structure and charge position effect on adsorption by aluminium hydroxide
Adsorption
aluminium hydroxide
peptide analogues
solubility and adsorption
structure and adsorption
charge position and adsorption
title_short Peptide solubility, structure and charge position effect on adsorption by aluminium hydroxide
title_full Peptide solubility, structure and charge position effect on adsorption by aluminium hydroxide
title_fullStr Peptide solubility, structure and charge position effect on adsorption by aluminium hydroxide
title_full_unstemmed Peptide solubility, structure and charge position effect on adsorption by aluminium hydroxide
title_sort Peptide solubility, structure and charge position effect on adsorption by aluminium hydroxide
dc.creator.fl_str_mv Trujillo, Mary
Valencia, Jesus
Calvo, Julio
dc.contributor.author.spa.fl_str_mv Trujillo, Mary
Valencia, Jesus
Calvo, Julio
dc.subject.proposal.spa.fl_str_mv Adsorption
aluminium hydroxide
peptide analogues
solubility and adsorption
structure and adsorption
charge position and adsorption
topic Adsorption
aluminium hydroxide
peptide analogues
solubility and adsorption
structure and adsorption
charge position and adsorption
description Solubility, structure and position of charges in a peptide antigen sequence can be mentioned as being amongst the basic features of adsorption. In order to study their effect on adsorption, seven analogue series were synthesized from a MSP-1 peptide sequence by systematically replacing each one of the positions in the peptide sequence by aspartic acid, glutamic acid, serine, alanine, asparagine, glutamine or lysine. Such modifications in analogue peptide sequences showed a non-regular tendency regarding solubility and adsorption data. Aspartic acid and Glutamic acid analogue series showed great improvements in adsorption, especially in peptides where Lysine in position 6 and Arginine in position 13 were replaced. Solubility of position 5 analogue was greater than the position 6 analogue in Aspartic acid series; however, the position 6 analogue showed best adsorption results whilst the Aspartic acid in position 5 analogue showed no adsorption in the same conditions. Nuclear Magnetic Resonance structural analysis revealed differences in the -helical structureextension between these analogues. The Aspartic acid in position 6, located in the polar side of the helix, may allow this analogueto fit better onto the adsorption regions suggesting that the local electrostatic charge is responsible for this behavior.
publishDate 2006
dc.date.issued.spa.fl_str_mv 2006
dc.date.accessioned.spa.fl_str_mv 2019-06-25T20:34:56Z
dc.date.available.spa.fl_str_mv 2019-06-25T20:34:56Z
dc.type.spa.fl_str_mv Artículo de revista
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url https://repositorio.unal.edu.co/handle/unal/22326
http://bdigital.unal.edu.co/13360/
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dc.relation.spa.fl_str_mv http://revistas.unal.edu.co/index.php/rcolquim/article/view/854
dc.relation.ispartof.spa.fl_str_mv Universidad Nacional de Colombia Revistas electrónicas UN Revista Colombiana de Química
Revista Colombiana de Química
dc.relation.ispartofseries.none.fl_str_mv Revista Colombiana de Química; Vol. 35, núm. 2 (2006); 135-146 0120-2804
dc.relation.references.spa.fl_str_mv Trujillo, Mary and Valencia, Jesus and Calvo, Julio (2006) Peptide solubility, structure and charge position effect on adsorption by aluminium hydroxide. Revista Colombiana de Química; Vol. 35, núm. 2 (2006); 135-146 0120-2804 .
dc.rights.spa.fl_str_mv Derechos reservados - Universidad Nacional de Colombia
dc.rights.coar.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.rights.license.spa.fl_str_mv Atribución-NoComercial 4.0 Internacional
dc.rights.uri.spa.fl_str_mv http://creativecommons.org/licenses/by-nc/4.0/
dc.rights.accessrights.spa.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv Atribución-NoComercial 4.0 Internacional
Derechos reservados - Universidad Nacional de Colombia
http://creativecommons.org/licenses/by-nc/4.0/
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
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dc.publisher.spa.fl_str_mv Universidad Nacional de Colombia
institution Universidad Nacional de Colombia
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