title: Modeling of active transport systems.
abstract: Transport proteins have critical physiological roles in nutrient transport and may be utilized as a mechanism to increase drug absorption. However, we have little understanding of these proteins at the molecular level due to the absence of high-resolution crystal structures. Numerous efforts have been made to characterize the P-glycoprotein efflux pump, the peptide transporter (PepT1) and the apical sodium-dependent transporter (ASBT) which are important not only for their native transporter function but also as drug targets to increase absorption and bioactivity. In vitro and computational approaches have been applied to gain some insight into these transporters with some success. This represents an opportunity for optimizing molecules as substrates for the solute transporters and providing a further screening system for drug discovery. Clearly the future growth in knowledge of transporter function will be led by integrated in vitro and in silico approaches.
authors.affiliation: Division of Pharmaceutics, The Ohio State University, 500 West 12th Avenue, Columbus, OH 43210-1291, USA.
authors.forename: Eric Y
authors.initials: EY
authors.lastname: Zhang
authors.forename: Mitch A
authors.initials: MA
authors.lastname: Phelps
authors.forename: Chang
authors.initials: C
authors.lastname: Cheng
authors.forename: Sean
authors.initials: S
authors.lastname: Ekins
authors.forename: Peter W
authors.initials: PW
authors.lastname: Swaan
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001693:Biological Transport, Active / Q000502:physiology*; D002352:Carrier Proteins / Q000378:metabolism* / Q000502:physiology; D002462:Cell Membrane / Q000378:metabolism; D006801:Humans; D008954:Models, Biological; D008969:Molecular Sequence Data
chemical_list: D018528:ATP-Binding Cassette Transporters; D002352:Carrier Proteins