Investigation of spectrin binding to phospholipid vesicles using isoindole fluorescent probe. Thermal properties of the bound and unbound protein.

Fluorescence of isoindole probe covalently bound to spectrin from pig erythrocytes, and fluorescence of tryptophanyl residues were used to study spectrin interaction with phospholipid bilayers. Evidence would be provided for conformational changes of spectrin occurring upon its binding to lipid bilayers. Fluorescence quenching experiments allowed to determine thermal stability of the protein in bound and unbound state. Spectrin binding to lipids was shown to protect the protein against thermal denaturation.