Spectrofluorimetric studies on the binding of salicylic acid to bovine serum albumin using warfarin and ibuprofen as site markers with the aid of parallel factor analysis

Physically crosslinked hydrogels were developed via solvent casting methods using a temperature-sensitive polymer, poly( N-isopropylacrylamide- co-acrylic acid), and a therapeutic polymer, salicylate-based poly(anhydride-esters), to concurrently release salicylic acid and bovine serum albumin in a sustained manner. The physical interactions between the two polymer systems were confirmed using Fourier transform infrared spectroscopy. The crosslinked polymers were porous, thus able to encapsulate bovine serum albumin (23 wt%) and then released the protein in a sustained fashion over 96 h. Concurrently, the hydrogel releases salicylic acid in a sustained manner up to 120 h. Hydrogel systems were cytocompatible at relevant therapeutic concentrations. These hydrogel systems can be used for simultaneous delivery of salicylic acid and protein to achieve synergic effects.

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Study of Drug-Protein Binding by Affinity Chromatography: Interaction of Bovine Serum Albumin and Salicylic Acid

Journal of Pharmaceutical Sciences ◽

10.1002/jps.2600670737 ◽

1978 ◽

Vol 67 (7) ◽

pp. 1005-1008 ◽

Cited By ~ 28

Author(s):

Naomi I. Nakano ◽

Takayuki Oshio ◽

Yukio Fujimqto ◽

Takashi Amiya

Keyword(s):

Salicylic Acid ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Protein Binding ◽

Affinity Chromatography ◽

Bovine Serum ◽

Drug Protein Binding

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Study of Thermal Dynamics of Defatted Bovine Serum Albumin in D2O Solution by Fourier Transform Infrared Spectra and Evolving Factor Analysis

Applied Spectroscopy ◽

10.1366/000370207781745919 ◽

2007 ◽

Vol 61 (9) ◽

pp. 921-927 ◽

Cited By ~ 13

Author(s):

Bo Yuan ◽

Koichi Murayama ◽

Huiming Yan

Keyword(s):

Factor Analysis ◽

Fourier Transform ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Ir Spectra ◽

Bovine Serum ◽

Fourier Transform Infrared ◽

State Transitions ◽

Thermal Dynamics ◽

Three Factor

Fourier transform infrared (FT-IR) spectra have been measured for defatted bovine serum albumin (BSA) in D2O with a concentration of 2.0 wt % over a temperature range of 26–90 °C and the corresponding difference spectra have been calculated by subtracting the contribution of D2O at the same temperature. Evolving factor analysis (EFA) by selecting two factors and three factors has been employed to analyze the temperature-dependent difference IR spectra in the 1700–1600 cm−1 spectral region of the defatted BSA in D2O solution. Three-factor EFA has been employed to determine the distinction of the three protein species involved in the process of temperature elevation: native, transitional, and denatured protein. The temperature profiles obtained from three-factor EFA indicate that heat-induced conformational change in the secondary structures of defatted BSA in D2O undergoes two two-state transitions, a drastic transition and a slight transition, which occur in the temperature ranges of 68–82 °C and 56–76 °C, respectively.

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