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dc.contributor.author
Deiber, Julio Alcides
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dc.contributor.author
Piaggio, María Virginia
dc.contributor.author
Peirotti, Marta Beatriz
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dc.date.available
2016-12-13T14:25:38Z
dc.date.issued
2014-03
dc.identifier.citation
Deiber, Julio Alcides; Piaggio, María Virginia; Peirotti, Marta Beatriz; Global chain properties of an all L-alpha-eicosapeptide with a secondary alpha -helix and its all retro D-inverso-alpha-eicosapeptide estimated through the modeling of their CZE determined electrophoretic mobilities; Wiley; Electrophoresis; 35; 5; 3-2014; 755-761
dc.identifier.issn
0173-0835
dc.identifier.uri
http://hdl.handle.net/11336/9248
dc.description.abstract
Several global chain properties of relatively long peptides composed of 20 amino acid residues are estimated through the modeling of their experimental effective electrophoretic mobilities determined by CZE for 2 < pH < 6. In this regard, an all L-alpha-eicosapeptide, including a secondary alpha-helix (Peptide 1) and its all retro D-inverso-alpha-eicosapeptide (Peptide 2), are considered. Despite Peptides 1 and 2 are isomeric chains, they do not present similar global conformations in the whole range of pH studied. These peptides may also differ in the quality of BGE components chain interactions depending on the pH value. Three Peptide 1 fragments (Peptides 3, 4, and 5) are also analyzed in this framework with the following purposes: (i) visualization of the effects of initial and final strands at each side of the alpha-helix on the global chain conformations of Peptide 1 at different pHs and (ii) analysis of global chain conformations of Peptides 1 and 2, and Peptide 1 fragments in relation to their pI values. Also, the peptidemaximum andminimum hydrations predicted by the model, compatible with experimental effective electrophoretic mobilities at different pHs, are quantified and discussed, and needs for further research concerning chain hydration are proposed. It is shown that CZE is a useful analytical tool for peptidomimetic designs and purposes.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
L-Alpha-Eicosapeptide
dc.subject
Peptide Effective Electrophoretic Mobility
dc.subject
Peptide Global Chain Properties
dc.subject
Peptidomimetic Structure-Function
dc.subject
Retro D-Alpha-Peptide
dc.subject.classification
Otras Ingeniería Química
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dc.subject.classification
Ingeniería Química
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dc.subject.classification
INGENIERÍAS Y TECNOLOGÍAS
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dc.title
Global chain properties of an all L-alpha-eicosapeptide with a secondary alpha -helix and its all retro D-inverso-alpha-eicosapeptide estimated through the modeling of their CZE determined electrophoretic mobilities
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-12-12T13:47:34Z
dc.journal.volume
35
dc.journal.number
5
dc.journal.pagination
755-761
dc.journal.pais
Alemania
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dc.journal.ciudad
Weinheim
dc.description.fil
Fil: Deiber, Julio Alcides. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química (i); Argentina
dc.description.fil
Fil: Piaggio, María Virginia. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas; Argentina
dc.description.fil
Fil: Peirotti, Marta Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Santa Fe. Instituto de Desarrollo Tecnológico para la Industria Química (i); Argentina
dc.journal.title
Electrophoresis
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1002/elps.201300395
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/elps.201300395/abstract
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