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

the immune protection-inducing protein structure concept in the search for steric-electron and topochemical principles for complete fully-protective chemically synthesised vaccine development

Manuel Elkin Patarroyo, Adriana Bermúdez, Martha Patricia Alba, Magnolia Vanegas, Armando Moreno-Vranich, Luis Antonio Poloche, Manuel Alfonso Patarroyo

Resultado de la investigación: Contribución a RevistaArtículo

16 Citas (Scopus)

Resumen

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-DRβ1*-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, non-interfering, long-lasting, protection-inducing, multi-epitope, multistage, minimal subunit-based chemically-synthesised peptides can be designed against diseases scourging humankind.

Idioma originalEnglish (US)
Páginas (desde-hasta)e0123249
PublicaciónPLoS One
Volumen10
N.º4
DOI
EstadoPublished - abr 16 2015
Publicado de forma externa

Huella dactilar

vaccine development
protein structure
Vaccines
electrons
peptides
Electrons
Peptides
Aotus (Cebidae)
Atoms
Proteins
immunoassays
epitopes
Haplorhini
monkeys
Epitopes
Assays
immune response

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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: the immune protection-inducing protein structure concept in the search for steric-electron and topochemical principles for complete fully-protective chemically synthesised vaccine development",
abstract = "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 ±3.5{\AA} 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-DRβ1*-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, non-interfering, long-lasting, protection-inducing, multi-epitope, multistage, minimal subunit-based chemically-synthesised peptides can be designed against diseases scourging humankind.",
author = "Patarroyo, {Manuel Elkin} and Adriana Berm{\'u}dez and Alba, {Martha Patricia} and Magnolia Vanegas and Armando Moreno-Vranich and Poloche, {Luis Antonio} and Patarroyo, {Manuel Alfonso}",
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AU - Patarroyo, Manuel Elkin

AU - Bermúdez, Adriana

AU - Alba, Martha Patricia

AU - Vanegas, Magnolia

AU - Moreno-Vranich, Armando

AU - Poloche, Luis Antonio

AU - Patarroyo, Manuel Alfonso

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AB - 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-DRβ1*-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, non-interfering, long-lasting, protection-inducing, multi-epitope, multistage, minimal subunit-based chemically-synthesised peptides can be designed against diseases scourging humankind.

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