Ainphipols are low molecular weight (<20 kDa) linear polymers having a distribution of polar and hydrophobic side chains which confers amphipaticity to the polymer. Amphipols represent a unique way of solubilizing integral membrane proteins. Amphipols wrap themselves around the hydrophobic transmembrane domains of membrane proteins so that the hydrophobic side chains of the polymer stabilize the hydrophobic surface of the protein, while the polar side chains of the polymer confer aqueous solubility to the protein-amphipol complex In Phase I a new and simpler route to the only existing family of amphipols was developed and an entirely new and potentially useful family of amphipols was discovered. In Phase II we plan to synthesize and characterize a number of variations of this family (called PMALT). These new molecules will be evaluated in the laboratory of Dr. Charles R. Sanders for their ability to solublize, stabilize, and maintain the functionality of membrane proteins. The study will provide the basis for future unique applications of amphipols in structural biology biochemistries, biomedicine, and biotechnology.
The possibility of using the materials proposed here to study membrane protein structure in solution via NMR is especially appearing. Amphipols may also provide the basis for new approaches in drug delivery, biosensors, and other biomedical/ technological applications. Presently, there is no commercial source for amphipol- class polymers. Anatrace has a history of timely introduction of new, useful detergent and other biochemicals to the international technical community.
