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The P-Glycoprotein (ABCB1) is a linker domain that causes multidrug resistance in tumor cells selected with lipophilic anticancer drugs. ABCB1 helps in encoding high-affinity binding sequences to [alpha]- and [beta]-tubulins and hence can be used in various tumor cells.

Photolabeling studies show that recombinant rat Mrp6 ABC transporter protein, expressed in Pichia pastoris, is stable and binds and hydrolyzes ATP. The differences in the properties between rMrp6 and the ABC transporter multidrug resistance associated protein 1 (MRP1) can be employed to understand the functional aspects of mutation in pseudoxanthoma elasticum patients.

Research has been conducted on the multidrug resistance-associated protein 1 (MRP1). The high-level expression and functional characterization of MRP1 in methylotrophic yeast Pichia pastoris has been carried out.

Results demonstrate that rhodamine 123 directly binds to three sites in the N- and C-domains of the multidrug resistance protein1 of Staphylococcus aureus as revealed by photoreactive-iodinated analogue IAARh123.

Research has been conducted on the P-glycoprotein and the multidrug resistance protein (MPR). Results indicate that MPR mediates the cytoxic natural product transport.

The study synthesized and characterized a novel photoreactive azido analogue of leucotriene (LTC4) (AALTC4). The results demonstrate a high-resolution map of LTC4 binding domains in multidrug resistance protein 1 (MRP1) and provide the first direct evidence for LTC4 binding within membrane multiple spanning domain of MRP1 (MSD0).

Results demonstrate that the glutathione analogue photoaffinity label interacts with the multidrug resistance protein 1, MRP1, at transmembrane 10-11 and 16-17 domains and cytoplasmic linker regions L0 and L1. The binding of labeled glutathione analogues mimicks that of unmodified glutathione, suggesting the precise binding location of glutathione within MRP1.