http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Divsalar, A.,Saboury, A.A.,Mansoori-Torshizi, H.,Hemmatinejad, B. Korean Chemical Society 2006 Bulletin of the Korean Chemical Society Vol.27 No.11
The interaction between whey carrier protein $\beta$-lactoglobulin type A and B (BLG-A and -B) and 2,2'-bipyridin n-hexyl dithiocarbamato Pd(II) nitrate (BPHDC-Pd(II)), a new heavy metal complex designed for anticancer property, was investigated by fluorescence spectroscopy combined with chemometry and circular dichroism (CD) techniques. A strong fluorescence quenching reaction of BPHDC-Pd(II) to BLG-A and -B was observed. Hence, BPHDC-Pd(II) complex can be bound to both BLG-A and -B, and quench the fluorescence spectra of the proteins. The quenching constant was determined using the modified Stern-Volmer equation. The binding parameters were evaluated by fluorescence quenching method. The results of binding study provided evidences presence of two and three sets of binding sites on the BLG-B and -A, respectively, for BPHDC-Pd(II) complex. Using fluorescence spectroscopy and chemometry, the ability of BLG-A and -B to form an intermediate upon interaction with BPHDC-Pd(II) complex was assessed. CD studies displayed that under influence of different concentrations of BPHDC-Pd(II) complex, the regular secondary structure of BLG-B had no significant changes, whereas for BLG-A a transition from $\alpha$-helix to $\beta$-structure was appeared. The results for both of BLG-A and -B displayed that BPHDC-Pd(II) complex can induce a conformational transition from the native form to an intermediate state with a slightly opened conformation, which is detectable with chemometry analyses.
A. Divsalar,A. A. Saboury*,H. Mansoori-Torshizi,B. Hemmatinejad 대한화학회 2006 Bulletin of the Korean Chemical Society Vol.27 No.11
The interaction between whey carrier protein b-lactoglobulin type A and B (BLG-A and -B) and 2,2'-bipyridin n-hexyl dithiocarbamato Pd(II) nitrate (BPHDC-Pd(II)), a new heavy metal complex designed for anticancer property, was investigated by fluorescence spectroscopy combined with chemometry and circular dichroism (CD) techniques. A strong fluorescence quenching reaction of BPHDC-Pd(II) to BLG-A and -B was observed. Hence, BPHDC-Pd(II) complex can be bound to both BLG-A and -B, and quench the fluorescence spectra of the proteins. The quenching constant was determined using the modified Stern-Volmer equation. The binding parameters were evaluated by fluorescence quenching method. The results of binding study provided evidences presence of two and three sets of binding sites on the BLG-B and -A, respectively, for BPHDC-Pd(II) complex. Using fluorescence spectroscopy and chemometry, the ability of BLG-A and -B to form an intermediate upon interaction with BPHDC-Pd(II) complex was assessed. CD studies displayed that under influence of different concentrations of BPHDC-Pd(II) complex, the regular secondary structure of BLG-B had no significant changes, whereas for BLG-A a transition from a-helix to b-structure was appeared. The results for both of BLG-A and -B displayed that BPHDC-Pd(II) complex can induce a conformational transition from the native form to an intermediate state with a slightly opened conformation, which is detectable with chemometry analyses.
( Adeleh Divsalar ),( Ali A. Saboury ),( Leila Ahadi ),( Elham Zemanatiyar ),( Hassan Mansouri Torshizi ) 생화학분자생물학회 (구 한국생화학분자생물학회) 2010 BMB Reports Vol.43 No.11
The biological evaluation of a new synthesized Pt(II)-complex, 2,2`-bipyridin Butylglycinato Pt(II) nitrate, an anti-tumor component, was studied at different temperatures by fluorescence and far UV circular dichroism (CD) spectroscopic methods. Human serum albumin (HSA) and human tumor cell line K562 were as targets. The Pt(II)-complex has a strong ability to quench the intrinsic fluorescence of HSA. Binding and thermodynamic parameters of the interaction were calculated by fluorescence quenching method. Far-UV-CD results showed that Pt(II)-complex induced increasing in content of α helical structure of the protein and stabilized it. The 50% cytotoxic concentration (Cc50) of complex was determined using MTT (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide) assay at different incubation times. Also, fluorescence staining with DAPI (4,6-diamidino-2-phenylindole) revealed some typical nuclear changes, which are characteristic of apoptosis. Above results suggest that Pt (II) complex is a promising anti-proliferative agent and should execute its biological effects by inducing apoptosis. [BMB reports 2010; 43(11): 766-771]
A New Approach for Thermodynamic Study on the Binding of Human Serum Albumin with Cerium Chloride
G. Rezaei Behbehani,A. Divsalar,A. A. Saboury,F. Faridbod,M. R. Ganjali 대한화학회 2009 Bulletin of the Korean Chemical Society Vol.30 No.6
Thermodynamics of the interaction between Cerium (III) chloride, Ce3+, with Human Serum Albumin, HSA, was investigated at pH 7.0 and 27 oC in phosphate buffer by isothermal titration calorimetry. Our recently solvation model was used to reproduce the enthalpies of HSA interaction by Ce3+. The solvation parameters recovered from our new model, attributed to the structural change of HSA and its biological activity. The interaction of HSA withCe3+ showed a set of two binding sites with negative cooperativity. Ce3+ interacts with multiple sites on HSA naffecting its biochemical and biophysical properties
A New Approach for Thermodynamic Study on the Binding of Human Serum Albumin with Cerium Chloride
Rezaei Behbehani, G.,Divsalar, A.,Saboury, A.A.,Faridbod, F.,Ganjali, M.R. Korean Chemical Society 2009 Bulletin of the Korean Chemical Society Vol.30 No.6
Thermodynamics of the interaction between Cerium (III) chloride, $Ce^{3+}$, with Human Serum Albumin, HSA, was investigated at pH 7.0 and $27\;{^{\circ}C}$ in phosphate buffer by isothermal titration calorimetry. Our recently solvation model was used to reproduce the enthalpies of HSA interaction by $Ce^{3+}$. The solvation parameters recovered from our new model, attributed to the structural change of HSA and its biological activity. The interaction of HSA with $Ce^{3+}$ showed a set of two binding sites with negative cooperativity. $Ce^{3+}$ interacts with multiple sites on HSA affecting its biochemical and biophysical properties.
A Product Inhibition Study on Adenosine Deaminase by Spectroscopy and Calorimetry
Saboury, Ali Akbar,Divsalar, Adeleh,Jafari, Ghasem Ataie,Moosavi-Movahedi, Ali Akbar,Housaindokht, Mohammad Reza,Hakimelahi, Hosain 생화학분자생물학회 2002 Journal of biochemistry and molecular biology Vol.35 No.3
Kinetic and thermodynamic studies have been made on the effect of the inosine product on the activity of adenosine deaminase in a 50 mM sodium phosphate buffer, pH 7.5, at $27^{\circ}C$ using UV spectrophotometry and isothermal titration calorimetry (ITC). A competitive inhibition was observed for inosine as a product of the enzymatic reaction. A graphical-fitting method was used for determination of the binding constant and enthalpy of inhibitor binding by using isothermal titration microcalorimetry data. The dissociation-binding constant is equal to $140\;{\mu}M$ by the microcalorimetry method, which agrees well with the value of $143\;{\mu}M$ for the inhibition constant that was obtained from the spectroscopy method.
H. Mansouri-Torshizi,M. Saeidifar,A. Divsalar,A. A. Saboury,S. Shahraki 대한화학회 2010 Bulletin of the Korean Chemical Society Vol.31 No.2
We report the preparation and characterization of a new and water soluble complex of palladium(II) with 1,10- phenanthroline and butyldithiocarbamate ligands. This compound has been studied through spectroscopic techniques, 1H NMR,IR, electronic spectra and elemental analysis and conductivity measurements. The complex shows 50% cytotoxic concentration (Ic50) value against chronic myelogenous leukemia cell line, K562, much lower than that of cisplatin. Thus the mode of binding of this complex to calf thymus DNA have been extensively investigated by isothermal titration UV-visible spectrophotometry, fluorescence, gel filteration and other methods. UV-visible studies show that the complex exhibits cooperative binding with DNA and remarkably denatures the DNA at extremely low concentration (~13μM). Fluorescence studies indicate that the complex intercalate into DNA. Gel filtration studies suggest that the binding of Pd(II) complex with DNA is strong enough that it does not readily break. In these interaction studies, several thermodynamic and binding parameters are also determined which may reflect the mechanism of action of this type of compound with DNA.
A. Hekmat, A. A. Saboury,A. Divsalar,M. Khanmohammadi 대한화학회 2008 Bulletin of the Korean Chemical Society Vol.29 No.8
Results of intrinsic and extrinsic fluorescence studies on choline oxidase revealed that the enzyme at high alkaline pH values has more accessible hydrophobic patches relative to acidic pH. Fluorescence quenching studies with acrylamide confirm these changes. The quenching constants were also determined at different pH(s) by using the Stern-Volmer equation. CD studies showed that at higher pH a transition from α-helix to β- structure was appeared while at lower pH the content of α-helix structure was increased. Furthermore, analysis of the spectral data using chemometric method gave evidence for existence of intermediate components at very high pH(s). Results of thermal denaturation evaluated that the enzyme has the most instability at higher pH(s). Altogether low and high pH values caused significant alteration on secondary and tertiary structures of choline oxidase via inducing of an intermediate.
Mansouri-Torshizi, H.,Saeidifar, M.,Divsalar, A.,Saboury, A.A.,Shahraki, S. Korean Chemical Society 2010 Bulletin of the Korean Chemical Society Vol.31 No.2
We report the preparation and characterization of a new and water soluble complex of palladium(II) with 1,10- phenanthroline and butyldithiocarbamate ligands. This compound has been studied through spectroscopic techniques, $^1H$ NMR, IR, electronic spectra and elemental analysis and conductivity measurements. The complex shows 50% cytotoxic concentration ($Ic_{50}$) value against chronic myelogenous leukemia cell line, K562, much lower than that of cisplatin. Thus the mode of binding of this complex to calf thymus DNA have been extensively investigated by isothermal titration UV-visible spectrophotometry, fluorescence, gel filteration and other methods. UV-visible studies show that the complex exhibits cooperative binding with DNA and remarkably denatures the DNA at extremely low concentration ($~13\;{\mu}M$). Fluorescence studies indicate that the complex intercalate into DNA. Gel filtration studies suggest that the binding of Pd(II) complex with DNA is strong enough that it does not readily break. In these interaction studies, several thermodynamic and binding parameters are also determined which may reflect the mechanism of action of this type of compound with DNA.
Assessment of hemolytic activity of bee venom against some physicochemical factors
Yaser Yousefpoor,Amir Amani,Adeleh Divsalar,Seyyedeh Elaheh Mousavi,Yaser Eskandari Torbaghan,Omid Emami 한국응용곤충학회 2019 Journal of Asia-Pacific Entomology Vol.22 No.4
Bee venom (BV) is a biotoxin with biologically active peptides which have cell lysis and hemolytic activity properties. These properties can be affected under different storage conditions or during the production process. In present study, we investigated effects of a number of physicochemical factors, including temperature, pH, UV radiation, ultrasound waves and storage time on hemolytic activity of BV. Maximum absorption and melting temperature of BV solution were obtained as 280 nm and ~70 °C, respectively. Cell hemolysis 50 (CH 50 ) -concentration of BV that can lyse 50% of red blood cells- was determined as 0.94 μg/ml at ambient temperature. CH 50 was shown not to be importantly varied at temperature up to 60 °C, pH value 2 to 13 and under UV/ ultrasound radiation. Storage at −20, 6 and 25 °C for 6 months made about 2.5, 35 and 1000 times increase in CH 50 . From the results, it may be concluded that BV is a relatively resistant hemolytic agent and can be used in a variety of laboratory research and product manufacturing methods.