INVESTIGADORES
CHIRDO Fernando Gabriel
artículos
Título:
P31-43 Gliadin Peptide forms Oligomers compatible with the monomer´s structure. Commentary
Autor/es:
BARRERA E; CHIRDO F.G; PANTANO S
Revista:
FRONTIERS IN IMMUNOLOGY
Editorial:
Frontiers Media SA
Referencias:
Año: 2019
ISSN:
1664-3224
Resumen:
In our recent publication p31-43 Gliadin Peptide Forms Oligomers and Induces NLRP3 Inflammasome/Caspase 1- Dependent Mucosal Damage in Small Intestine? (1) we showed by a combination of experimental and simulation techniques that the peptide p31-43 gliadin has an intrinsic propensity to form oligomers, which trigger the NLRP3 inflammasome, resulting in intestinal inflammation and pathology. In particular, molecular simulations performed with the SIRAH force field (2), showed that isolated p31-43 peptides exhibit a broad conformational dynamic with some PPII component, mostly related to the presence of Pro36 and Pro42. Simulation of multiple replicas showed a spontaneous tendency to aggregation with a concomitant increase in the PPII content for Pro38 and Pro 39.
