Behaviour of the bovine brain phosphatidylethanolamine binding protein at the air/water interface

• Published in: Materials Science & Engineering C 1999-12, Vol.8, p.43-46
• Main Authors: Maget-Dana, Régine, Bureaud, Nicole, Schoentgen, Françoise
• Format: Article
• Language: English
• Subjects: Air/water interface; Analytical, structural and metabolic biochemistry; Binding and carrier proteins; Biological and medical sciences; Bovine brain Phosphatidylethanolamine binding protein (PEBP); Fundamental and applied biological sciences. Psychology; Protein adsorption; Protein monomolecular films; Proteins
• ISSN: 0928-4931; 1873-0191
• DOI: 10.1016/S0928-4931(99)00006-5

The cytosolic bovine brain PEBP is a basic protein of 21 kDa devoid of disulfide bridges. It has been shown to form stable monomolecular protein films at the air/water interface. In the course of time, the PEBP films expanded nearly three times probably as the result of protein unfolding at the interface. The PEBP diffusion from a protein solution towards the interface is very low in account of its high content in polar residues and of its widely β-sheet structure. The adsorption rate of PEBP at the air/water interface is dependent on the bulk concentration of the protein and the saturation of the surface occurs as early as the bulk concentration reaches 2.5×10 −6 M in amino acid. The surface concentration of PEBP at saturation is less than 2×10 18 amino acid/m 2, a value in a 10 lower range than observed for other proteins of the same size and devoid of disulfide bridges.