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PubMed1983

The interaction between pancreatic lipase and colipase: a protein-protein interaction regulated by a lipid.

Pancreatic lipase readily adsorbs to a triglyceride droplet. In the intestine the triglyceride droplets are covered with bile salt and phospholipids which will prevent the adsorption of lipase. In this situation the activity of lipase is restored by colipase, another pancreatic protein. Lipase and colipase in solution form a 1:1 molar complex. I emphasize the fact that the binding and conformation of the two proteins in the complex is dependent on the type of lipids present and suggest that this lipid-determined structure of the complex is responsible for the actual function of lipase/colipase. It determines whether colipase assists lipase in binding to the bile salt-covered triglyceride droplet as is the case with tributyrin as substrate, and whether colipase in addition activates lipase as is the case with a mixed trioctanoin/lecithin monolayer substrate. In other words, lipase activity is regulated by the combined action of colipase and the lipid substrate.

Colipases↗
PubMed1991

Characterization of the interaction of doxorubicin with (poly)phosphoinositides in model systems. Evidence for specific interaction with phosphatidylinositol-monophosphate and -diphosphate.

The anticancer drug doxorubicin penetrates into Langmuir monolayers containing phosphoinositides. Upon binding of doxorubicin to phosphoinositide-containing SUV, its fluorescence is self-quenched due to self-association. As compared to other anionic phospholipids, as much as 2- to 3-fold larger effects were obtained with PIP and PIP2, in mixtures of these lipids with DOPC. Doxorubicin competes efficiently with the non-penetrating antibiotic neomycin for binding to PIP2. According to its penetration, specific binding of doxorubicin was half-maximal at 5-15 microM. It is likely that also in biological membranes doxorubicin binds specifically to PIP and PIP2.

Doxorubicin↗