New Photoactivators for Multiphoton Excited Three-dimensional Submicron Cross-linking of Proteins: Bovine Serum Albumin and Type 1 Collagen¶†

A new Cd(II) complex, [Cd(H4pbidc)(H2O)] n (1), incorporating 2,2′-(propane-1,3-diyl)bis(1H- imidazole-4,5-dicarboxylic acid) (H6pbidc) was synthesized and characterized by elemental analysis, infrared spectra and X-ray single-crystal diffraction. In complex 1, each Cd(II) ion is hepta-coordinated, showing a significantly distorted pentagonal-bipyramidal coordination environment. Adjacent Cd(II) ions are alternately joined through two carboxylate oxygen atoms and two bridging water molecules resulting in a one-dimensional chain structure. In the solid state, adjacent chains are further linked by hydrogen bonds, forming a three-dimensional supramolecular architecture. Meanwhile, the interactions of complex 1 with bovine serum albumin were analysed by fluorescence measurements under physiological conditions. The results indicated that the fluorescence intensity of bovine serum albumin was decreased considerably upon the addition of complex 1 through a static quenching mechanism with formation of one binding site. The negative values of the thermodynamic parameters including enthalpy change (Δ H), entropy change (Δ S) and Gibbs free energy change (Δ G) showed that hydrogen bonding and van der Waals forces were the main interactions in the binding of complex 1 to bovine serum albumin, and the binding process is spontaneous in thermodynamics.

Download Full-text

Combined cross-linking treatments of bovine serum albumin gel beadlets for controlled-delivery of caffeine

Food Hydrocolloids ◽

10.1016/j.foodhyd.2008.09.009 ◽

2009 ◽

Vol 23 (5) ◽

pp. 1398-1405 ◽

Cited By ~ 15

Author(s):

Chee-Yuen Gan ◽

Lai-Hoong Cheng ◽

Eng-Tong Phuah ◽

Pei-Ni Chin ◽

Abbas F.M. AlKarkhi ◽

...

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Controlled Delivery ◽

Cross Linking

Download Full-text

Two Dimensional and Three Dimensional Interactions between Bovine Serum Albumin and Chondroitin Sulfate

Polymer Journal ◽

10.1295/polymj.pj2006123 ◽

2007 ◽

Vol 39 (4) ◽

pp. 298-303 ◽

Cited By ~ 3

Author(s):

Shouhong Xu ◽

Masakatsu Yonese

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Chondroitin Sulfate ◽

Bovine Serum ◽

Three Dimensional ◽

Two Dimensional

Download Full-text

No association between anti-bovine serum albumin antibodies and islet cell reactive antibodies in newly diagnosed type 1 diabetic patients

Diabetes Research and Clinical Practice ◽

10.1016/0168-8227(94)90137-6 ◽

1994 ◽

Vol 26 (1) ◽

pp. 35-41 ◽

Cited By ~ 4

Author(s):

F. Lühder ◽

M. Schlosser ◽

D. Michaelis ◽

B. Ziegler ◽

K.-D. Kohnert ◽

...

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Islet Cell ◽

Diabetic Patients ◽

Newly Diagnosed ◽

Type 1 Diabetic Patients

Download Full-text

The Study on the Interaction Conditions of Water-Soluble Chitosan with Bovine Serum Albumin

Advanced Materials Research ◽

10.4028/www.scientific.net/amr.347-353.1281 ◽

2011 ◽

Vol 347-353 ◽

pp. 1281-1286

Author(s):

Shan Shan Huang ◽

Feng Zuo Qu ◽

Tong Kuan Xu ◽

Li Cui

Keyword(s):

Bovine Serum Albumin ◽

Fluorescence Quenching ◽

Serum Albumin ◽

Linear Relationship ◽

Binding Constant ◽

Bovine Serum ◽

Fluorescence Spectra ◽

Three Dimensional ◽

Water Soluble ◽

Visible Absorption

The interaction conditions between the water-soluble chitosans(WSC) and bovine serum albumin (BSA) was studied by Ultraviolet-visible absorption and fluorescence spectrometries. It was shown there was a good linear relationship between the absorbency A and the BSA concentration(0~1.5g/L) and WSC concentration (0~1.5 g/L). The fluorescence quenching of WSC to BSA was static quenching. When the temperature is 30°C, its binding constant Ka=5.35×104 L/mol, binding site n=1.05. The influence of WSC on the conformation of BSA was analyzed by sychronous fluorescence spectra and three-dimensional fluorescence spectrum.

Download Full-text