جستجوی مقالات مرتبط با کلیدواژه "circular dichroism spectroscopy" در نشریات گروه "زیست شناسی"

According to the importance of coumarin derivatives as an effective medication on cancer cells and various other therapeutic effects, in this study we investigated the effect of a new derivative of coumarin named 3- (tetrazol-5-yl) coumarin on single-stranded DNA by different spectroscopic methods in solution.

The present study has investigated the effect of 3- (tetrazol-5-il) coumarin on single-stranded DNA in vitro. The findings demonstrates that the rate of single strand DNA absorption enhances by interaction with 3-(tetrazol-5-yl) coumarin at 210 and 260 nm. The fluorescence intensity of single-stranded DNA increases in a concentration-dependent of 3- (tetrazol-5-yl) coumarin, indicating the binding of 3- (tetrazol-5-yl) coumarin to the chromophores in single-stranded DNA.

Binding of 3- (tetrazol-5-yl) coumarin to single-stranded DNA causes a significant increase in ellipticity in circular dichroism of DNA molecules in the regions of 220 and 275 nm which is more positive at 245 nm. The results indicate a stronger binding of 3- (tetrazol-5-l) coumarin to single-stranded DNA, which may be due to the fact that single-stranded DNA may be more available during replication.

The results obtained from the effect of 3- (tetrazol-5-yl) coumarin on single-stranded DNA can provide valuable information to design medications by coumarin derivatives which have more anti-tumor effect and less side effects.

Human alpha1-antitrypsin is a glycoprotein comprised of 394 amino acids and 52 kDa molecular weight, which is mostly synthesized and secreted by hepatocytes, diffuses to interstitial lung tissues, and has an essential function to protected tissues against neutrophil elastase. One of the significant challenges in dealing with alpha-1-antitrypsin is the structural instability of the folded form of protein and, consequently, the accumulation of polymers in lung tissue. This makes patients vulnerable to chronic obstructive pulmonary disease, severe asthma, and emphysema. Intravenous augmentation therapy of alpha 1-antitrypsin is one of the most prevalent therapies. Moreover, patients who are candidates for that have respiratory symptoms, and the use of bronchodilator (Salbutamol) is the first recommended standard treatment. In this study, protein purification was performed by using high-performance affinity chromatography and, its purity was confirmed by gel electrophoresis. The effect of different concentrations of salbutamol on heat-induced polymerization at 60 ° C was investigated by non-denaturing polyacrylamide gel electrophoresis, dynamic light scattering (DLS), and circular dichroism (CD) techniques. Protein activity was measured by trypsin inhibitor capacity (TIC) assay. The results indicated that salbutamol decreases the rate of polymerization by reducing the flexibility of the reactive center loop, thus decelerate protein activity reduction. Therefore, salbutamol can be an appropriate supplementary for alpha 1-antitrypsin and a proper option for the treatment of protein polymerization associated diseases.