Binding of selected phenolic compounds to proteins.
In the context of this study, the noncovalent binding of selected phenolic compounds (chlorogenic, ferulic, and gallic acids, quercetin, rutin, and isoquercetin) to different proteins (human serum albumin, bovine serum albumin, soy glycinin, and lysozyme) was studied with direct (Hummel-Dreyer/size exclusion chromatography) and/or indirect methods (fluorescence absorbance properties of the binding components). In the latter case, the measurement of the phenol binding was achieved by exploiting the intrinsic fluorescence emission properties of quercetin as a probe. From the data obtained, the binding constants and the number of binding sites were calculated. The binding parameters were influenced by different factors, where, e.g., increasing temperature and ionic strength as well as decreasing pH cause a diminished binding. The structures of the proteins as determined by circular dichroism indicate changes in the tertiary structure with the secondary structure remaining intact.
Rawel
Harshadrai M
HM
University of Potsdam, Institute of Nutritional Science, D-14558 Nuthetal, A.-Scheunert Allee 114-116, Germany. rawel@rz.uni-potsdam.de
Meidtner
Karina
K
Kroll
Jürgen
J
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002850:Chromatography, Gel; D003373:Coumaric Acids / Q000378:metabolism; D005916:Globulins / Q000378:metabolism; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008433:Mathematics; D009113:Muramidase / Q000378:metabolism; D009994:Osmolar Concentration; D010636:Phenols / Q000378:metabolism*; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D011794:Quercetin / Q000378:metabolism; D012709:Serum Albumin / Q000378:metabolism; D030262:Soybean Proteins
D003373:Coumaric Acids; D005916:Globulins; D010636:Phenols; D011506:Proteins; D012709:Serum Albumin; D030262:Soybean Proteins; C011474:glycinin; D011794:Quercetin; C004999:ferulic acid; D009113:Muramidase