IMPIPS : The Immune Protection-Inducing Protein Structure concept in the search for steric-electron and topochemical principles for complete fully-protective chemically synthesised vaccine development
Determining immune protection-inducing protein structures (IMPIPS) involves defining the stereo-electron and topochemical characteristics which are essential in MHC-p-TCR complex formation. Modified high activity binding peptides (mHABP) were thus synthesised to produce a large panel of IMPIPS measu...
Autores Principales: | , , , , , , |
---|---|
Formato: | Artículo (Article) |
Lenguaje: | Inglés (English) |
Publicado: |
2015
|
Materias: | |
Acceso en línea: | http://repository.urosario.edu.co/handle/10336/19030 https://doi.org/10.1371/journal.pone.0123249 |
id |
ir-10336-19030 |
---|---|
recordtype |
dspace |
spelling |
ir-10336-190302022-08-25T21:34:30Z IMPIPS : The Immune Protection-Inducing Protein Structure concept in the search for steric-electron and topochemical principles for complete fully-protective chemically synthesised vaccine development Patarroyo, Manuel Elkin Bermudez, Adriana Alba, Martha Patricia Vanegas, Magnolia Moreno-Vranich, Armando Poloche, Luis Antonio Patarroyo, Manuel A. Proteína de unión epítopo Antígeno Hla Dr Hidrógeno Vacuna contra la malaria Nitrógeno Oxígeno Prolina Cloruro de sodio Péptido sintético Vacuna recombinante Animal Experiment Modelo animal Reacción de anticuerpo de antígeno Aoto Sitio de unión Estudio controlado Estructura de la droga Electrón Enlace de hidrógeno Estructura proteica inductora de protección inmunitaria Respuesta inmune inmunoensayo inmunogenicidad Malaria No humano Virulencia del parásito Síntesis de péptidos Química Física Plasmodium falciparum Enlace proteico Estructura de la proteína Animal Chemistry Haplorhin Conformación de proteínas Biología Inmunología Proteínas portadoras Antígenos Synthetic Vaccines Proline Synthetic Peptide Sodium Chloride Recombinant Vaccine Animal Model Animal Experiment Antigen Antibody Reaction Aotus Binding Site Controlled Study Drug Structure Electron Hydrogen Bond Immune Protection Inducing Protein Structure Immune Response Immunoassay Binding Protein Epitope Hla Dr Antigen Hydrogen Malaria Vaccine Oxygen Immunogenicity Nonhuman Parasite Virulence Peptide Synthesis Physical Chemistry Plasmodium Falciparum Protein Binding Protein Structure Chemistry Protein Conformation Haplorhini Animals Electrons Nitrogen Determining immune protection-inducing protein structures (IMPIPS) involves defining the stereo-electron and topochemical characteristics which are essential in MHC-p-TCR complex formation. Modified high activity binding peptides (mHABP) were thus synthesised to produce a large panel of IMPIPS measuring 26.5 ±3.5Å between the farthest atoms fitting into Pockets 1 to 9 of HLA-DRβ1∗structures. They displayed a polyproline II-like (PPIIL) structure with their backbone O and N atoms orientated to establish H-bonds with specific residues from HLA-DRβ∗-peptide binding regions (PBR). Residues having specific charge and gauche+ orientation regarding p3χ1, p5χ2, and p7χ1 angles determined appropriate rotamer orientation for perfectly fitting into the TCR to induce an appropriate immune response. Immunological assays in Aotus monkeys involving IMPIPS mixtures led to promising results; taken together with the aforementioned physicochemical principles, noninterfering, long-lasting, protection-inducing, multi-epitope, multistage, minimal subunit-based chemically-synthesised peptides can be designed against diseases scourging humankind. © 2015 Patarroyo et al. 2015 2019-02-08T19:45:56Z info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 1932-6203 http://repository.urosario.edu.co/handle/10336/19030 https://doi.org/10.1371/journal.pone.0123249 eng info:eu-repo/semantics/openAccess application/pdf instname:Universidad del Rosario |
institution |
EdocUR - Universidad del Rosario |
collection |
DSpace |
language |
Inglés (English) |
topic |
Proteína de unión epítopo Antígeno Hla Dr Hidrógeno Vacuna contra la malaria Nitrógeno Oxígeno Prolina Cloruro de sodio Péptido sintético Vacuna recombinante Animal Experiment Modelo animal Reacción de anticuerpo de antígeno Aoto Sitio de unión Estudio controlado Estructura de la droga Electrón Enlace de hidrógeno Estructura proteica inductora de protección inmunitaria Respuesta inmune inmunoensayo inmunogenicidad Malaria No humano Virulencia del parásito Síntesis de péptidos Química Física Plasmodium falciparum Enlace proteico Estructura de la proteína Animal Chemistry Haplorhin Conformación de proteínas Biología Inmunología Proteínas portadoras Antígenos Synthetic Vaccines Proline Synthetic Peptide Sodium Chloride Recombinant Vaccine Animal Model Animal Experiment Antigen Antibody Reaction Aotus Binding Site Controlled Study Drug Structure Electron Hydrogen Bond Immune Protection Inducing Protein Structure Immune Response Immunoassay Binding Protein Epitope Hla Dr Antigen Hydrogen Malaria Vaccine Oxygen Immunogenicity Nonhuman Parasite Virulence Peptide Synthesis Physical Chemistry Plasmodium Falciparum Protein Binding Protein Structure Chemistry Protein Conformation Haplorhini Animals Electrons Nitrogen |
spellingShingle |
Proteína de unión epítopo Antígeno Hla Dr Hidrógeno Vacuna contra la malaria Nitrógeno Oxígeno Prolina Cloruro de sodio Péptido sintético Vacuna recombinante Animal Experiment Modelo animal Reacción de anticuerpo de antígeno Aoto Sitio de unión Estudio controlado Estructura de la droga Electrón Enlace de hidrógeno Estructura proteica inductora de protección inmunitaria Respuesta inmune inmunoensayo inmunogenicidad Malaria No humano Virulencia del parásito Síntesis de péptidos Química Física Plasmodium falciparum Enlace proteico Estructura de la proteína Animal Chemistry Haplorhin Conformación de proteínas Biología Inmunología Proteínas portadoras Antígenos Synthetic Vaccines Proline Synthetic Peptide Sodium Chloride Recombinant Vaccine Animal Model Animal Experiment Antigen Antibody Reaction Aotus Binding Site Controlled Study Drug Structure Electron Hydrogen Bond Immune Protection Inducing Protein Structure Immune Response Immunoassay Binding Protein Epitope Hla Dr Antigen Hydrogen Malaria Vaccine Oxygen Immunogenicity Nonhuman Parasite Virulence Peptide Synthesis Physical Chemistry Plasmodium Falciparum Protein Binding Protein Structure Chemistry Protein Conformation Haplorhini Animals Electrons Nitrogen Patarroyo, Manuel Elkin Bermudez, Adriana Alba, Martha Patricia Vanegas, Magnolia Moreno-Vranich, Armando Poloche, Luis Antonio Patarroyo, Manuel A. IMPIPS : The Immune Protection-Inducing Protein Structure concept in the search for steric-electron and topochemical principles for complete fully-protective chemically synthesised vaccine development |
description |
Determining immune protection-inducing protein structures (IMPIPS) involves defining the stereo-electron and topochemical characteristics which are essential in MHC-p-TCR complex formation. Modified high activity binding peptides (mHABP) were thus synthesised to produce a large panel of IMPIPS measuring 26.5 ±3.5Å between the farthest atoms fitting into Pockets 1 to 9 of HLA-DRβ1∗structures. They displayed a polyproline II-like (PPIIL) structure with their backbone O and N atoms orientated to establish H-bonds with specific residues from HLA-DRβ∗-peptide binding regions (PBR). Residues having specific charge and gauche+ orientation regarding p3χ1, p5χ2, and p7χ1 angles determined appropriate rotamer orientation for perfectly fitting into the TCR to induce an appropriate immune response. Immunological assays in Aotus monkeys involving IMPIPS mixtures led to promising results; taken together with the aforementioned physicochemical principles, noninterfering, long-lasting, protection-inducing, multi-epitope, multistage, minimal subunit-based chemically-synthesised peptides can be designed against diseases scourging humankind. © 2015 Patarroyo et al. |
format |
Artículo (Article) |
author |
Patarroyo, Manuel Elkin Bermudez, Adriana Alba, Martha Patricia Vanegas, Magnolia Moreno-Vranich, Armando Poloche, Luis Antonio Patarroyo, Manuel A. |
author_facet |
Patarroyo, Manuel Elkin Bermudez, Adriana Alba, Martha Patricia Vanegas, Magnolia Moreno-Vranich, Armando Poloche, Luis Antonio Patarroyo, Manuel A. |
author_sort |
Patarroyo, Manuel Elkin |
title |
IMPIPS : The Immune Protection-Inducing Protein Structure concept in the search for steric-electron and topochemical principles for complete fully-protective chemically synthesised vaccine development |
title_short |
IMPIPS : The Immune Protection-Inducing Protein Structure concept in the search for steric-electron and topochemical principles for complete fully-protective chemically synthesised vaccine development |
title_full |
IMPIPS : The Immune Protection-Inducing Protein Structure concept in the search for steric-electron and topochemical principles for complete fully-protective chemically synthesised vaccine development |
title_fullStr |
IMPIPS : The Immune Protection-Inducing Protein Structure concept in the search for steric-electron and topochemical principles for complete fully-protective chemically synthesised vaccine development |
title_full_unstemmed |
IMPIPS : The Immune Protection-Inducing Protein Structure concept in the search for steric-electron and topochemical principles for complete fully-protective chemically synthesised vaccine development |
title_sort |
impips : the immune protection-inducing protein structure concept in the search for steric-electron and topochemical principles for complete fully-protective chemically synthesised vaccine development |
publishDate |
2015 |
url |
http://repository.urosario.edu.co/handle/10336/19030 https://doi.org/10.1371/journal.pone.0123249 |
_version_ |
1743431047489519616 |
score |
12,131701 |