Análisis in silico a nivel proteico de la estructura de presenilina-1 en homínidos.

Introduction. Amyloid plaques are one of the neuropathological markers of Alzheimer's disease, formed by peptide fragments that are deposited, derived from the protease cut of the enzyme γ-secretase, of which presenilin-1 is the subunit with the active site, it is possible to investigate at the evolutionary level what happens with this protein in a sample of hominids. Materials and methods. structural biology study is carried out to evaluate changes in the structure of the proteins modeled with the Phyre2 software and primary sequence alignments with Jalview from the hominids Pongo abelii, Pan troglodytes, Pan paniscus, Gorilla gorilla, Homo sapiens and two species used in biological tests as Macaca fascicularis, Macaca mulatta. Results. It was found that the primary sequences of isoform 467 presented very high percentages of identity with T-Coffee 2.0 of 99.57 % on average, within its primary sequence in the pairwise alignment and at the three-dimensional level, with the Needleman- Wunsch algorithm, slight changes were found in the structure at the loop level, but very conserved between species, which was also reflected in standard deviation values of the models of less than 5 Å. Conclusions. Finally, no significant changes were found at the structural level in the protein with protease function, so for the hominin sample there were no evolutionary changes, at least for this protein, and in perspective, the other components of the enzyme gamma-secretase remain to evaluate. [ABSTRACT FROM AUTHOR]