IMBICE   05372
INSTITUTO MULTIDISCIPLINARIO DE BIOLOGIA CELULAR
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Binding properties of Sterol Carrier Protein 2 (SCP2) from Yarrowia lipolytica characterized using Laurdan
Autor/es:
ERMÁCORA, MARIO R.; GIANOTTI, ALEJO R.; FERREYRA, RAUL G.
Lugar:
La Plata
Reunión:
Congreso; XLVII Reunión Anual de la Sociedad Argentina de Biofísica; 2018
Institución organizadora:
Sociedad Argentina de Biofísica
Resumen:
Sterol Carrier Protein 2 (SCP2) binds lipids with high affinity and broad specificity, and is present in all forms of life, as a stand-alone protein or as module in a large variety of multidomain proteins, playing different roles. In this work we characterized the hydrophobicity, fluidity, and dipolar dynamics of the binding site of SCP2 from Yarrowia lipolytica using the environmentally sensitive fluorescent probe Laurdan. The fluorescence properties of bound Laurdan revealed a binding site with an overall polarity similar to that of dichloromethane and an internal phase comparable to that of phospholipid membranes with coexisting solid-ordered and liquid-crystalline states. Moreover, the binding site of SCP2 can accommodate competitively more than one ligand, with micro and nanomolar dissociation constants. Our findings are important for the characterization of SCP2 biological functions and the design of specific inhibitors.