The role of pi-interactions and hydrogen bonds in fully protective synthetic malaria vaccine development

Analysis of our Plasmodium falciparum malaria parasite peptides’ 1H-NMR database in the search for H-bonds and ?-interactions led us to correlate their presence or absence with a peptide's particular immunological behavior. It was concluded that a 26.5 ± 1.5 Å between positions 1 to 9 of the HL...

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Autores:

Tipo de recurso:

Fecha de publicación:

2017

Institución:

Universidad del Rosario

Repositorio:

Repositorio EdocUR - U. Rosario

Idioma:

eng

OAI Identifier:

oai:repository.urosario.edu.co:10336/23516

Acceso en línea:

https://doi.org/10.1016/j.bbrc.2017.01.077
https://repository.urosario.edu.co/handle/10336/23516

Palabra clave:

HLA DRB1 antigen
Malaria vaccine
HLA antigen class 2
Malaria vaccine
Peptide
Protein binding
Recombinant vaccine
Animal experiment
Animal model
Antibody titer
Aotus
Article
Conformation
Force
Hydrogen bond
Immune response
Immunity
Immunofluorescence
Major histocompatibility complex
Molecular docking
Molecular interaction
Nonhuman
Peptide synthesis
Ph
Pi interaction
Priority journal
Proton nuclear magnetic resonance
Static electricity
Binding site
Chemistry
Drug design
Hydrogen bond
Procedures
Protein analysis
Protein conformation
Sequence analysis
Structure activity relation
Ultrastructure
Binding Sites
Drug Design
Histocompatibility Antigens Class II
HLA-DRB1 Chains
Hydrogen Bonding
Malaria Vaccines
Peptides
Protein Binding
Protein Conformation
Protein Interaction Mapping
Structure-Activity Relationship
Hydrogen bond
Malaria
TCR-peptide-MHC complex
X—H-? interaction
Synthetic
Protein
Sequence Analysis
Vaccines

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