Ponente
Descripción
Protein immobilization is defined as the process by which the degrees of freedom of movement of proteins are completely or partially restricted, through their binding or confinement in the space of a solid surface. Recently, with the aim of optimizing the immobilization processes, a rational design strategy for immobilized derivatives (RDID) has been developed. The neutral aminopeptidase from M1 family of Escherichia coli (ePepN) is a non-essential cytosolic enzyme that has a high degree of similarity to several aminopeptidases from pathogenic microorganisms, becoming it in a very attractive target for the development of new antimicrobial drugs. Based on this, the aim of this work was to predict the stability of the ePepN covalently immobilized on glyoxyl-Sepharose CL supports using the RDID strategy. The protein under study retained most of its enzymatic activity at pH 8.0 and 9.0 after 24 hours of incubation. Six possible clusters were identified, among them 1, 2 and 6 contain the N-terminus, which presents the highest reactivity of the residues under study for all the pH values used in the prediction. At pH 8.0, the most likely configurations for the immobilized derivatives presented a high probability of unipoint binding to the support. The deviation angles were calculated and cluster 6 was the most catalytically favored. As the pH under study increased, a sharp increase in the probability of multipoint interaction was observed and therefore an increase in the stability of the immobilized derivatives is expected. A decrease in the immobilized derivative functional competence is expected, though.
- del Monte-Martínez, A., B. Cutiño, D. Gil, L. Mokarzel, J. Gonzalez, M. Pupo, M.A.Chavez, T. Pons and J. Diaz (2010) Rational design strategy in the synthesis of derivatives immobilized. Its implementation through the RDID1.0 program. Cient Univ Cienc Inf series (Cuba). 3(3):185–202.
- González-Bacerio, J., R. Fando, A. Del Monte-Martínez, J. Charli y M. Chávez (2014). Plasmodium falciparum M1-aminopeptidase: A promising target for the development of antimalarials. Curr. Drug Targets. 15: 1144-1165.
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