Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 1 de 1
Filter
Add more filters










Database
Language
Publication year range
1.
Int J Biol Macromol ; 61: 373-8, 2013 Oct.
Article in English | MEDLINE | ID: mdl-23928012

ABSTRACT

The main aim of this study is to provide understanding for the interaction modes and the binding affinity based on the study of PEG 400 that binds to ctDNA. The effects of the PEG-400-to-ctDNA ratio, pH, incubation time and thermal stability of ctDNA on PEG-ctDNA biocomplex formation were studied. UV-vis-NIR absorption analysis indicated that PEG forms a complex with ctDNA via a mechanism other than intercalation. The results of thermal denaturation studies showed that the PEG-ctDNA biocomplex helix was stabilised, with a resulting increase in the PEG-ctDNA melting temperature. FTIR analysis indicated that the PEG binds to ctDNA through weak to moderately strong hydrophilic and hydrophobic interactions with the base pairs of ctDNA. TEM micrographs showed that the addition of PEG to ctDNA caused ctDNA to condense with PEG molecules into an irregular aggregate structure. These results demonstrate that the PEG-ctDNA biocomplex has potential applications in biomedical sciences.


Subject(s)
DNA/chemistry , Polyethylene Glycols/chemistry , Animals , Cattle , Macromolecular Substances/chemistry , Macromolecular Substances/ultrastructure , Molecular Conformation , Spectroscopy, Near-Infrared , Thermodynamics
SELECTION OF CITATIONS
SEARCH DETAIL
...