Conformational states of annexin VI in solution induced by acidic pH

FEBS Letters

Bandorowicz-Pikula, Joanna¹  Golczak, Marcin¹  Kirilenko, Aneta¹  Pikula, Slawomir¹ 

[1] Department of Cellular Biochemistry, Nencki Institute of Experimental Biology, 3 Pasteur Street, 02-093 Warsaw, Poland

关键词: Annexin VI;    Steady-state fluorescence;    Circular dichroism;    pH-induced folding;    Anx;    annexin;    CD;    circular dichroism;    FRET;    fluorescence resonance energy transfer;    PtdSer;    phosphatidylserine;    SDS–PAGE;    sodium dodecyl sulfate–polyacrylamide gel electrophoresis;    TNS;    2-(p-toluidino)naphthalene-6-sulfonic acid;   

DOI  :  10.1016/S0014-5793(01)02402-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Acidic pH-induced folding of annexin (Anx)VI in solution was investigated in order to study the mechanism of formation of ion channels by the protein in membranes. Using 2-(p-toluidino)naphthalene-6-sulfonic acid as a hydrophobic probe, it was demonstrated that AnxVI exerts a large change in hydrophobicity at acidic pH. Moreover, circular dichroism spectra indicated that the native state of AnxVI changes at acidic pH towards a state characterized by a significant loss of α-helix content and appearance of new β-structures. These changes are reversible upon an increase of pH. It is postulated that the structural folding of AnxVI could explain how a soluble protein may undergo transition into a molecule able to penetrate the membrane hydrophobic region. The physiological significance of these observations is discussed.

【 授权许可】

Unknown