Dna Interaction with Human Serum Albumin Studied by Affinity Capillary Electrophoresis and Ftir Spectroscopy.
From: Department of Chemistry-Biology, University of Québec at Trois-Rivières, Canada.
DNA and cell biology
- Publish Date: Jan 2006
- ISSN: 1044-5498
- Volume: 25
- Issue: 1
- Pages: 63-8
- Medium: Print
- Language: English
- Citation (JAMA): Malonga H, Neault J F, Arakawa H, et al. Dna Interaction with Human Serum Albumin Studied by Affinity Capillary Electrophoresis and Ftir Spectroscopy.. DNA Cell Biol. Jan 2006;25:63-8
Abstract
The question addressed in this study is how does the protein-DNA complexation affect the structure and dynamics of DNA and protein in aqueous solution. We examined the interaction of calf-thymus DNA with human serum albumin (HSA) in aqueous solution at physiological conditions, using constant DNA concentration of 12.5 mM (phosphate) and various HSA contents 0.25 to 2% or 0.04 to 0.3 mM. Affinity capillary electrophoresis and FTIR spectroscopic methods were used to determine the protein binding mode, the association constant, sequence preference, and the biopolymer secondary structural changes in the HSA-DNA complexes. Spectroscopic evidence showed two types of HSA-DNA complexes with strong binding of K(1) = 4.5 x 10(5) M(-1) and weak binding of K(2) = 6.10 x 10(4) M(-1). The two major binding sites were located on the G-C bases and the backbone PO(2) group. The protein-DNA interaction stabilizes the HSA secondary structure. A minor alteration of B-DNA structure was observed, while no major protein conformational changes occurred.
Mesh Headings (Keywords): Animals, Binding Sites, Cattle, DNA, Electrophoresis, Capillary, Humans, Models, Molecular, Nucleic Acid Conformation, Protein Binding, Protein Conformation, Serum Albumin, Spectroscopy, Fourier Transform Infrared
Check for Full Text / PubMed Unique Identifier (PMID): 16405401
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