Molecular modeling of the phosphoglycerate kinase and fructose-bisphosphate aldolase proteins from Candida glabrata and Candida albicans

Candida species are considered one of the most common fungal pathogens affecting humans. The first colonization stage of these pathogens is based on their adhesion to the host's cells, which is mediated by cell wall proteins (CWP), such as the moonlight-like CWP. Among the latter, the fructose-bisphosphate aldolase (Fba1) and the phosphoglycerate kinase (Pgk) are of particular relevance because it has been found that, in Candida species, they participate in the response to several virulence and/or pathogenicity factor. These characteristics allow us to propose the Fba1 and Pgk as possible candidates to be used as therapeutic targets in treating candidiasis. Notwithstanding, to demonstrate that these enzymes are useful as therapeutic targets, it is crucial to know the tridimensional structure (3D) of both proteins to then perform in silico assays that will allow identifying possible inhibitors of these enzymes. In these sense, there are several experimental techniques that provide detailed information about the three-dimensional (3D) structure of proteins. However, sometimes these techniques can pose some difficulties in obtaining crystallized proteins in sufficient amounts and of good quality. Hence, computational methods are determinant for predicting structures and identifying and valorizing potential targets of pharmaceutical drugs. In this sense, however, these experimental techniques have not yielded the 3D structures of the Fba1 and Pgk proteins of C. albicans and C. glabrata. Therefore, this work aimed to perform structural studies of the Fba1 and Pgk of C. albicans and C. glabrata through modeling and molecular dynamics, obtaining theoretical models of their interaction with potential drugs using bioinformatics tools. Based on them, computational approaches have led to theoretical models of their interaction with other drugs.