Gold and colloidal gold surface influence on dna conformational change

DNA conformational changes caused by gold and colloidal gold surface have been studied by surface enhanced infrared spectroscopy (SEIRA), spectroscopy of plasmon resonance (SPR), atomic force microscopy (AFM) and principal component analysis. Experimental data have shown that DNA conformation is slightly influenced by gold surface, while it is strongly altered by colloidal gold. Spectroscopic features of DNA-colloidal gold system have shown that the intensity of the asymmetric PO₂– band at 1240 cm⁻¹ decreases by two times, and that of symmetric band at 1090 cm⁻¹ decreases by 2.4 times whereas the halfwidth of phosphate bands increases by 35–40 cm⁻¹; a frequency shift of asymmetric band position from 1240 to 1246 cm⁻¹ and a symmetric band from 1090 to 1106 cm⁻¹ has been observed. It was shown that intensity variation and shift of DNA base vibrations together with the broadening of OH, NH, and CH stretching vibrations occur due to DNA conformational changes and the redistribution of the H-bonding network. A supposition about DNA condensation by colloidal gold was made. SEIRA and AFM data have showed major DNA structural changes occurred on gold colloidal particles. It was found that all the spectral features are more prominent for DNA–colloidal gold system deposited on gold substrate than on CaF₂ substrate

Adsorption of mono- and multivalent cat- and anions on DNA molecules

Adsorption of monovalent and multivalent cat- and anions on a deoxyribose nucleic acid (DNA) molecule from a salt solution is investigated by computer simulation. The ions are modelled as charged hard spheres, the DNA molecule as a point charge pattern following the double-helical phosphate strands. The geometrical shape of the DNA molecules is modelled on different levels ranging from a simple cylindrical shape to structured models which include the major and minor grooves between the phosphate strands. The densities of the ions adsorbed on the phosphate strands, in the major and in the minor grooves are calculated. First, we find that the adsorption pattern on the DNA surface depends strongly on its geometrical shape: counterions adsorb preferentially along the phosphate strands for a cylindrical model shape, but in the minor groove for a geometrically structured model. Second, we find that an addition of monovalent salt ions results in an increase of the charge density in the minor groove while the total charge density of ions adsorbed in the major groove stays unchanged. The adsorbed ion densities are highly structured along the minor groove while they are almost smeared along the major groove. Furthermore, for a fixed amount of added salt, the major groove cationic charge is independent on the counterion valency. For increasing salt concentration the major groove is neutralized while the total charge adsorbed in the minor groove is constant. DNA overcharging is detected for multivalent salt. Simulations for a larger ion radii, which mimic the effect of the ion hydration, indicate an increased adsorbtion of cations in the major groove.Comment: 34 pages with 14 figure

DNA adducts with antioxidant flavonoids: Morin, apigenin, and naringin

Flavonoids have recently attracted a great interest as potential therapeutic drugs against a wide range of free-radical-mediated diseases. The anticancer and antiviral activities of these natural products are implicated in their mechanism of actions. While the antioxidant activity of these natural polyphenolic compounds is well known, their bindings to DNA are not fully investigated. This study was designed to examine the interactions of morin (Mor), naringin (Nar), and apigenin (Api) with calf thymus DNA in aqueous solution at physiological conditions, using constant DNA concentration (6.25 mM) and various drug/DNA(phosphate) ratios of 1/40 to 1. FTIR and UV-Vis spectroscopic methods were used to determine the ligand binding modes, the binding constant, and the stability of DNA in flavonoid-DNA complexes in aqueous solution. Spectroscopic evidence shows both intercalation and external binding of flavonoids to DNA duplex with overall binding constants of Kmorin = 5.99 � 103 M-1, Kapigenin = 7.10 � 104 M-1, and Knaringin = 3.10 � 103 M-1. The affinity of ligand-DNA binding is in the order of apigenin > morin > naringin. DNA aggregation and a partial B- to A-DNA transition occurs upon morin, apigenin, and naringin complexation. © Copyright 2008, Mary Ann Liebert, Inc

Design of functionalized folic acid–chitosan nanoparticles for delivery of tetracycline, doxorubicin, and tamoxifen

Design of functionalized folic acid–chitosan nanoparticles for delivery of tetracycline, doxorubicin, and tamoxife

Biomolecular study and conjugation of two paraaminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis.

Two aminobenzoic acid derivatives DAB-0 and DAB-1 showed distinct biological properties on murine bladder cancer (BCa) cell line MB49-I. In contrast to DAB-1, DAB-0 does not possess any anti-inflammatory activity and is less toxic. Furthermore, DAB-0 does not interfere with INFc-induced STAT1 activation and TNFa-induced IjB phosphorylation, while DAB-1 does. In order to rationalize these results, the binding efficacy of DAB-0 and DAB-1 with serum proteins such a human serum albumin (HSA), bovine serum albumin (BSA) and beta-lactoglobulin (b-LG) was investigated in aqueous solution at physiological pH. Multiple spectroscopic methods and thermodynamic analysis were used to determine the binding efficacy of DAB-0 and DAB-1 with serum proteins. Drug-protein conjugation was observed via through ionic contacts. DAB-1 forms stronger adducts than DAB-0, while b-LG shows more affinity with the order of stability b-LG>BSA>HSA. The stronger complexation of DAB-1 with serum proteins might account for its biological potential and transport in the blood. The binding efficacy ranged from 40 to 60%. Major alterations of protein secondary structures were detected upon drug complexation. Serum proteins are capable of delivering DAB-1 in vitro.Abbreviations: BSA: bovine serum albumin; DAB-0: N0-[4-(2,5-dioxo-pyrrolidin-1-yl)-benzoyl]-hydrazine carboxylic acid tert-butyl ester; DAB-1: N0-[4-(2,5-dioxo-2,5-dihydro-pyrrol-1-yl)-benzoyl]-hydrazine carboxylic acid tert-butyl est; FTIR: Fourier transform infrared; b-LG, beta-lactoglobulin; HAS: human serum albuminFil: Chanphai, P.. Université du Québec a Montreal; CanadáFil: Cloutier, F.. Université du Québec a Montreal; CanadáFil: Oufqir, Y.. Université du Québec a Montreal; CanadáFil: Leclerc, M.F.. Université du Québec a Montreal; CanadáFil: Eijan, Ana Maria. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Oncología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Reyes Moreno, C.. Université du Québec a Montreal; CanadáFil: Bérubé, G.. Université du Québec a Montreal; CanadáFil: Tajmir Riahi, H.A.. Université du Québec a Montreal; Canad