Calcofluor White - carbohydrate residues

In these three different studies, we are monitoring the same type of interaction calcofluor white - carbohydrate residues. 

Albani, J.R., Sillen, A., Coddeville, B., Plancke, Y.D. and Engelborghs, Y. (1999) Dynamics of carbohydrate residues of ai-acid glycoprotein (orosomucoid) followed by red-edge excitation spectra and emission anisotropy studies of Calcofluor White. Carbohydrate Research 322,87-94. 

The interaction between Calcofluor White and carbohydrate residues of a -acid glycoprotein depends on the secondary structure of the carbohydrate residues, with the fluorescence parameters of Calcofluor being sensitive to this spatial secondary structure. 

The values of of a cliromophore can change whether it is free in solution or bound to a protein. This change can be important or non-significant. For example we determined the value of of calcofluor white free in solution and bound to ai-acid glycoprotein which contains 40% carbohydrate by weight. Calcofluor White binds specifically to the hydrophilic carbohydrate residues (Albani and Plancke, 1998 1999), although interaction with hydrophobic pockets of some proteins such as serum albumin occurs also (Albani and Plancke, 1998 1999). 

Figure 8.39. Determination of the efficiency (E) of energy transfer from Trp residues of ai-acid glycoprotein to calcofluor white. The value of the efficiency determined at the extrapolation is equal to 0.45. Source Albani, J. R., 2003, Carbohydr. Res. 338, 2233-2236.

Albani. J. R, 2001, Effect of binding of calcofluor white on the carbohydrate residues of apacid glycoprotein (orosomucoid) on the structure and dynamics of the protein moiety. A fluorescence study. Carbohydrate Research. 334, 141-151. 

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