Protein-calixarene interactions: complexation of Bovine Serum Albumin by sulfonatocalix[n]arenes.
The complexation of Bovine Serum Albumin with sulfonatocalix[n]arenes has been demonstrated by means of electrospray mass spectrometry, dynamic light scattering and atomic force microscopy; with sulfonatocalix[4]arene one strong and two weaker binding sites are detected; the effects on the structure of thin films formed by surface deposition of BSA show that the sulfonatocalix[n]arenes act to reticulate the films and produce essentially planar systems.
Memmi
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Institut de Biologie et Chimie des Protéines, CNRS-UCBL1, UMR 5086, 7 passage du Vercors, Lyon, F69367, France.
Lazar
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A
Brioude
A
A
Ball
V
V
Coleman
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AW
D000818:Animals; D001952:Bridged-Ring Compounds / Q000378:metabolism*; D047250:Calixarenes; D002417:Cattle; D046911:Macromolecular Substances; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D021241:Spectrometry, Mass, Electrospray Ionization; D013451:Sulfonic Acids / Q000378:metabolism*; D020349:Surface Plasmon Resonance
D001952:Bridged-Ring Compounds; D046911:Macromolecular Substances; D013451:Sulfonic Acids; D047250:Calixarenes; D012710:Serum Albumin, Bovine