Mechanism by Which Cholesterol Induces Sphingomyelin Conformational Changes at an Air/Water Interface.

This work investigates the interactions in cholesterol and sphingomyelin monolayers at the molecular level by high-resolution broadband sum frequency generation vibrational spectroscopy (HR-BB-SFG-VS). The SFG spectra of natural egg sphingomyelin (ESM) as a function of cholesterol concentration are obtained at an air/water interface under different polarization combinations. The analysis of the spectra shows that cholesterol can induce sphingomyelin conformational changes at an air/water interface. The mechanism is proposed. When cholesterol is inserted into the ESM monolayer, the inherent intramolecular hydrogen bonds between the phosphate moiety and 3OH in the sphingosine backbones are destroyed. During this process, the sphingosine backbones become more ordered, while the conformation of the N-linked long acid chain remains unaltered. The OH of the cholesterol head group can bind to the -PO -2 of the ESM molecule, and the orientation of the -PO -2 in the head groups changes to be more parallel to the interface.