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
| Autor: | Manuel E. Patarroyo, Manuel A. Patarroyo, Luis A. Poloche, Martha Patricia Alba, Adriana Bermúdez, Magnolia Vanegas, Armando Moreno-Vranich |
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| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Síntesis de péptidos
Protein Conformation Sitio de unión Virulencia del parásito Biología Cloruro de sodio lcsh:Medicine Plasma protein binding Respuesta inmune No humano Sodium Chloride Physical Chemistry chemistry.chemical_compound Protein structure Vacuna contra la malaria Estructura de la droga Peptide synthesis Oxígeno lcsh:Science Proteínas portadoras Péptido sintético Immune Response Immunoassay Vaccines Synthetic Vaccines Multidisciplinary Aoto Nitrógeno Modelo animal Haplorhini Antígenos Aotus Immunogenicity Plasmodium Falciparum Antígeno Hla Dr Chemistry Immune Protection Inducing Protein Proteína de unión Enlace de hidrógeno Epitope Drug Structure Vacuna recombinante Research Article Protein Binding Steric effects Electrón inmunogenicidad Protein Structure Proline Stereochemistry Nitrogen Protein subunit Inmunología Electrons Biology Hidrógeno Estructura proteica inductora de protección inmunitaria Electron Prolina Reacción de anticuerpo de antígeno Hydrogen Bond Malaria Vaccine Malaria Vaccines inmunoensayo Hla Dr Antigen Synthetic Peptide Animals Química Física Controlled Study Binding site Peptide Synthesis Polyproline helix Animal Parasite Virulence Binding protein lcsh:R Synthetic Binding Site Structure Estudio controlado Animal Experiment Nonhuman Virology Conformación de proteínas Malaria Recombinant Vaccine Oxygen Antigen Antibody Reaction chemistry Haplorhin lcsh:Q Animal Model epítopo Enlace proteico Binding Protein Estructura de la proteína Hydrogen |
| Zdroj: | Murray, C.J., Rosenfeld, L.C., Lim, S.S., Andrews, K.G., Foreman, K.J., Haring, D., Global malaria mortality between 1980 and 2010: A systematic analysis (2012) Lancet, 379, pp. 413-431., PMID: 22305225 Repositorio EdocUR-U. Rosario Universidad del Rosario instacron:Universidad del Rosario PLoS ONE, Vol 10, Iss 4, p e0123249 (2015) PLoS ONE |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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