Presentation Title

Homology Modeling and Simulations of P-glycoprotein

Presenter Information

Exequiel PunzalanFollow
Yong BaFollow

Faculty Mentor

Yong Ba

Start Date

18-11-2017 2:15 PM

End Date

18-11-2017 3:15 PM

Location

BSC-Ursa Minor 37

Session

Poster 3

Type of Presentation

Poster

Subject Area

physical_mathematical_sciences

Abstract

P-glycoprotein (P-gp) is an ATP-binding transporter that indiscriminately binds and exports a wide array of drugs. It is believed that its overexpression in tumor cells is one of the main causes of multidrug resistance in these cells. Several crystal structures of proteins related to human P-gp have been solved in recent years. Since there is a lack of crystal structure for human P-gp, these homologous proteins are used as templates to build three-dimensional models of the inward and outward facing state of human P-gp. Docking and molecular dynamics simulations are incorporated to explore the behavior and binding mode of anticancer drugs such as chlorambucil-tempol in the generated homology models. These simulations can help refine our understanding of the binding and efflux mechanisms of P-gp on anticancer drugs.

This document is currently not available here.

Share

COinS
 
Nov 18th, 2:15 PM Nov 18th, 3:15 PM

Homology Modeling and Simulations of P-glycoprotein

BSC-Ursa Minor 37

P-glycoprotein (P-gp) is an ATP-binding transporter that indiscriminately binds and exports a wide array of drugs. It is believed that its overexpression in tumor cells is one of the main causes of multidrug resistance in these cells. Several crystal structures of proteins related to human P-gp have been solved in recent years. Since there is a lack of crystal structure for human P-gp, these homologous proteins are used as templates to build three-dimensional models of the inward and outward facing state of human P-gp. Docking and molecular dynamics simulations are incorporated to explore the behavior and binding mode of anticancer drugs such as chlorambucil-tempol in the generated homology models. These simulations can help refine our understanding of the binding and efflux mechanisms of P-gp on anticancer drugs.