Ricardo Aguilera García

 raguilera@udca.edu.co

GRUPOS DE INVESTIGACIÓN: PRODUCTOS NATURALES U.D.C.A

LÍNEAS DE INVESTIGACIÓN:   Modelación Matemática, Computacional y Aplicaciones

FACULTAD:  Ciencias

CATEGORÍA COLCIENCIAS:    

NIVEL DE FORMACIÓN: Maestría/Magister

Matemático, M.Sc Ingeniería de Sistemas. Docente en el área de Matemáticas e investigador en el área de Química, Modelación Matemáticas específicamente en el
Estudio a nivel molecular de la interacción péptidos-proteínas HLA (Antígenos leucocitarios humanos), Explorando la naturaleza de la interacción human class II MHC protein, HLA-DR1 (DRB*0101) y el virus de la influenza hemagglutinin peptide, HA306- 318, usando la función MEP ( the molecular electrostatic potential ) y la teoría QTAM ( Quantum Theory of Átomos in Molecules)

PRODUCTOS DESTACADOS

Exploring the nature of the H-bonds between the human class II MHC protein, HLA-DR1 (DRB*0101) and the influenza virus hemagglutinin peptide, HA306-318, using the quantum theory of atoms in molecules
Fecha de publicación: 02/01/2018


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Exploring the nature of the H-bonds between the human class II MHC protein, HLA-DR1 (DRB*0101) and the influenza virus hemagglutinin peptide, HA306-318, using the quantum theory of atoms in molecules
Fecha de publicación: 02/01/2018

The nature of the H-bonds between the human protein HLA-DR1 (DRB*0101) and the hemagglutinin peptide HA306-318 has been studied using the Quantum Theory of Atoms in Molecules for the first time. We have found four H-bond groups: one conventional CO··HN bond group and three nonconventional CO··HC, π··HC involving aromatic rings and HN··HCaliphatic groups. The calculated electron density at the determined H-bond critical points suggests the follow protein pocket binding trend: P1 (2,311) >> P9 (1.109) > P4 (0.950) > P6 (0.553) > P7 (0.213) which agrees and reveal the nature of experimental findings, showing that P1 produces by a long way the strongest binding of the HLA-DR1 human protein molecule with the peptide backbone as consequence of the vast number of H-bonds in the P1 area and at the same time the largest specific binding of the peptide Tyr308 residue with aromatic residues located at the binding groove floor. The present results suggest the topological analysis of the electronic density as a valuable tool that allows a non-arbitrary partition of the pockets binding energy via the calculated electron density at the determined critical points. © 2018, © 2018 Informa UK Limited, trading as Taylor & Francis Group.


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