eng
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
2016-07-01
2
1
1
7
21156
Pre-Clinical and Clinical Data Confirm the Anticancer Effect of Deuterium Depletion
Gabor Somlyai
gsomlyai@hyd.hu
1
Behnam Javaheri
behnamjavaheri69@gmail.com
2
Hadi Davari
3
Zoltán Gyöngyi
4
Ildikó Somlyai
5
Kirk A. Tamaddon
6
László G. Boros
7
HYD LLC for Cancer Research and Drug Development, Fürj u. 2, Budapest 1124, Hungary
Behnam Javaheri--Department of Biology, Science and Research branch, Islamic Azad University, Tehran, Iran.,Petro Parsian Pharmed Inc. Tehran, Iran.
The two stable isotopes of hydrogen, protium (1H) and deuterium (2H) differ in their physicochemical nature. Deuterium-depleted water (DDW) significantly inhibited the growth rate of different tumor cell lines in culture media and xenotransplanted MDA-MB-231, MCF-7 human breast adenocarcinomas and PC-3 human prostate tumors in vivo. The apoptosis-triggering effect of DDW was demonstrated both in vitro and in vivo. The anti-cancer effect of D-depletion was also confirmed in a double-blind, randomized, 4-month-long, human phase II clinical trial on prostate cancer. D-depletion, as an adjuvant, caused 3-7 fold increases of median survival time (MST) in lung cancer, two-fold in advanced breast cancer and it also effectively prevented recurrences of early stage breast cancer. It is suggested that the cell cycle regulating system is able to recognize the changes in the 2H/1H ratio. Two key events takes place in the cell at the same time: the binding of growth hormone to the receptor activates the H+-transport system, which preferentially eliminates H+, resulting in an increased 2H/1H ratio, which is essential to start cell division; the properly working mitochondria, the terminal complex of mitochondrial electron transport chain reducing molecular oxygen to DDW, which reduces the 2H/1H ratio and inhibits the cell growth. The balance between the activated H+-transport system and the DDW producing mitochondria which determine the 2H/1H ratio in the cells is proposed as the key mechanism to regulate cell growth.
https://www.bmmj.org/article_21156_8ce88e1fc4eb84273b093c1e7c8ebb03.pdf
Deuterium depleted water
DDW
Cell growth
Clinical
Cancer
eng
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
2016-07-01
2
1
8
20
23075
Protein Stability, Folding, Disaggregation and Etiology of Conformational Malfunctions
Ali Akbar Moosavi-Movahedi
moosavi@ut.ac.ir
1
Ali Akbar Saboury
saboury@ut.ac.ir
2
Saman Hosseinkhani
saman_h@modares.ac.ir
3
Azadeh Lohrasbi-Nejad
lohrasbinejad@icst.ac.ir
4
Mehran Habibi-Rezae
mhabibi@ut.ac.ir
5
Parvaneh Maghami
maghami.p@gmail.com
6
Maliheh Atri
m.atri@umz.ac.ir
7
Leila Fotouhi
l.fotouhi@ut.ac.ir
8
IBB, Universiy of Teharn
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran
Department of Biotechnology, Faculty of Agriculture, Shahid Bahonar University of Kerman, Kerman, Iran
School of Biology, College of Science, University of Tehran, Tehran, Iran
IBB, University of Tehran, Tehran, Iran
Department of Molecular & Cell Biology, Faculty of Basic Sciences, University of Mazandaran, Babolsar, Iran
IBB, University of Tehran, Tehran, Iran
Estimation of protein stability is important for many reasons: first providing an understanding of the basic thermodynamics of the process of folding, protein engineering, and protein stability plays important role in biotechnology especially in food and protein drug design. Today, proteins are used in many branches, including industrial processes, pharmaceutical industry, and medical fields. Activity and stability of proteins are essential for providing healthy condition or required during their production, storage and use in their applications. Through the first part of this review, we aim to define the protein stability terms and factors. Any factor induces stabilizing conformation and/or aggregation of proteins might be of importance in etiology of the conformational diseases. In the second part we are going to clarify a comprehensive definition of protein stability issues with special emphasis on the advantages of these concepts in protein conformational diseases and biotechnology with a short insight to protein engineering approaches.
https://www.bmmj.org/article_23075_675cb3e5bea0f3f80b02624f482c9ac9.pdf
Protein stability
Conformational diseases
Reversibility
Refolding
Protein aggregation
eng
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
2016-07-01
2
1
21
27
21157
Association of Polymorphism at 3׳-UTR of Urokinase Gene with Risk of Calcium Kidney Stones
Neda Assari
assari_69@yahoo.com
1
SeiedAbdolmajid Angaji
angaji@khu.ac.ir
2
Saeed Morovvati
morovvati@hotmail.com
3
Department Of cell and Molecular biology, Kharazmi University
Department of Molecular and Biology, Faculty of Medical Sciences, Baghiyatallah University of Medical Sciences, Tehran, Iran
Urokinase might play a role in the formation of kidney stones. This study was done to determine the association between +4065 T/C polymorphism at the 3′-untranslated region of urokinase gene and calcium kidney stones. This Case-Control study was carried out on 70 cases with a history of calcium kidney stones and 70 controls from the Baqiyatallah hospital of Tehran in 2013. The study of polymorphism was performed by Allele-specific PCR method. Mutant T allele frequency was %41 in cases and %18 in controls. Hardy-Weinberg equilibrium (HWE) was tested using chi-square test. The chi-square showed that the control population is in HWE, and as expected, the patient group does not follow HWE. The odds ratio for the risk of the T allele was 1.7 (%95 confidence interval 0.2988-1.158). A significant association was found between the urokinase gene T/C polymorphism and the formation of calcium kidney stones. Also, effect modification was examined for both sexes and different age groups. According to the results, T polymorphism in the 3’-UTR of urokinase gene may increase with age.
https://www.bmmj.org/article_21157_4a8b1d25ff62021c47a0121c1d1bfecb.pdf
single nucleotide polymorphism
3'-Untranslated region
AS-PCR
Hardy-Weinberg equilibrium
eng
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
2016-07-01
2
1
28
33
21158
Designing a Label Free Aptasensor for Detection of Methamphetamine
Rezvan Kohzadi
rez1.kohzadi@gmail.com
1
Ahmad Molaeirad
molaeirad@gmail.com
2
Mahdi Alijanianzadeh
alijanianzadeh_m@yahoo.com
3
Nasrin Kamali
n_camali@yahoo.com
4
Mansour Mohtashamifar
moh1965@mut.ac.ir
5
1- Department of Bioscience and Biotechnology, Malek-Ashtar University of Technology, Tehran, Iran
1- Department of bioscience and biotechnology, Malek-Ashtar university of technology, Tehran, Iran
1- Department of Bioscience and Biotechnology, Malek-Ashtar University of Technology, Tehran, Iran
1- Department of Bioscience and Biotechnology, Malek-Ashtar University of Technology, Tehran, Iran
2- Electronic Research Center, Tehran, Iran
A label-free electrochemical nucleic acid aptasensor for the detection of methamphetamine (MA) by the immobilization of thiolated self-assembled DNA sequences on a gold nanoparticles-chitosan modified electrode is constructed. When MA was complexed specifically to the aptamer, the configuration of the nucleic acid aptamer switched to a locked structure and the interface of the biosensor changed, resulting in a variation of the corresponding peak current of an electrochemical probe ([Fe(CN)6]3-/4-). Two different methods of cyclic voltammetry (CV) and microcantilever were employed to determine MA detection limit. Under the optimized experimental conditions, the presented sensor exhibits a nice specificity towards MA. The detection limits for MA in electrode and microcantilever were obtained 10 and 0.7 nM. The proposed aptasensor can be easily regenerated by the denaturalization of aptamer-target complexes in a heated water bath at 80-90 °C. Besides, this biosensor has a high reproducibility and selectivity, which can be a promising method to detect MA in real samples.
https://www.bmmj.org/article_21158_2f5da8f45f9b96eca2b0f37f91d163ab.pdf
Aptasensor
Methamphetamine
Detection limit
eng
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
2016-07-01
2
1
34
43
21766
Isothermal Titration Calorimetry and Molecular Dynamics Simulation Studies on the Binding of Indometacin with Human Serum Albumin
Elham Mozaffari
elham_mozaffari@yahoo.com
1
Elham Tazikeh-lemeski
elham_tazike@yahoo.com
2
Ali Akbar Saboury
saboury@chamran.ut.ac.ir
3
Department of Chemistry, Gorgan Branch, Islamic Azad University, Gorgan, Iran
department of chemistry-gorgon branch-islamic ad university-gorgan-iran
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
Human serum albumin (HSA) is the most abundant protein in the blood plasma. Drug binding to HSA is crucial to study the absorption, distribution, metabolism, efficiency and bioavailability of drug molecules. In this study, isothermal titration calorimetry and molecular dynamics simulation of HSA and its complex with indometacin (IM) were performed to investigate thermodynamics parameters and the structural changes induced by the ligand binding, respectively. To estimate the binding affinity of drug molecule to subdomains IB and IIA in HSA protein, binding free energies were calculated using the Molecular Mechanics Poisson-Boltzmann Surface Area (MM-PBSA). The binding association constant (Ka) and the standard Gibbs free energy changes (G) of indometacin binding to the protein obtained from ITC technique are 9.12 103 M-1 and -5422 Kcal mol-1, respectively. All results indicate that the binding affinity of the drug molecule to subdomain IIA is more than that of subdomain IB of HSA. Thus the obtained thermodynamics characteristics, hydrophobic forces most likely played a major role, but hydrogen bonding also could not be ignored. One of the most important finding is that the subdomain IIA of HSA is the main binding site for indomethacin that confirmed by molecular dynamics simulation.
https://www.bmmj.org/article_21766_13b99402c9b90b79b6c94d2a44f12b4d.pdf
Human serum albumin (HSA)
Isothermal titration calorimetry (ITC)
Molecular dynamics simulation (MD)
Indomethacin (IM)
Molecular mechanics poisson-boltzmann surface area (MM-PBSA)
eng
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
2016-07-01
2
1
44
52
21799
Evaluation of Different Functionalized CNTs for Development of Choline Amperometric Biosensor
Sharareh Sajjadi
sajadi@riau.ac.ir
1
Hedayatollah Ghourchian
hadi@ibb.ut.ac.ir
2
Parvaneh Rahimi
rahimi.parvaneh@gmail.com
3
Roudehen Branch, Islamic Azad University, Roudehen, Iran
University of Tehran, IBB
University of Tehran
Choline oxidase (ChOx) was chosen as a model enzyme for evaluating the performance of CNTs’ functional groups for development of enzyme electrodes. CNTs were functionalized with carboxylic acid, amine or amide groups. Carboxylic acid, amine and amide functionalized CNTs were obtained by acid treatment, ethylenediamine or tetraethylenepentamine chemically modification and ammonia plasma treatment, respectively. The CNTs with different functional groups were mixed with 1-butyl-3-methylimidazolium tetrafluoroborate as a typical room temperature ionic liquid. ChOx was adsorbed on the thus prepared nanocomposites containing different modified electrodes and its electron transfer and electroanalytical response towards choline was investigated. The resulting data showed that the ammonia plasma treated nanocomposite had higher apparent heterogeneous electron transfer rate constant (2.74 s-1) than the others, indicating more facile and rapid rates of electron transfer; while, nanocomposites modified with tetraethylenepentamine functionalized CNTs showed the most sensitive response towards choline (1.09×103 A M-1 m-2) with the lowest detection limit of 5.81×10-6 M. Consequently, tetraethylenepentamine modified electrodes were more convenient for choline biosensing applications.
https://www.bmmj.org/article_21799_ea798a5ba32d773fd76331cae05307e2.pdf
Carbon nanotubes
Functionalization
Ionic liquid
Choline oxidase
eng
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
2016-07-01
2
1
53
58
21800
Immobilization of Subtilisin Carlsberg on Modified Silica Gel by Cross-linking and Covalent Binding Methods
Tayebeh Nazari
nazari_t25@yahoo.com
1
Mahdi Alijanianzadeh
alijanianzadeh_m@yahoo.com
2
Ahmad Molaeirad
molaeirad@gmail.com
3
Maryam Khayati
khayati293@yahoo.com
4
Department of Bioscience and Biotechnology, Malek-Ashtar University of Technology, Tehran, Iran
Department of Bioscience and Biotechnology, Malek Ashtar University of Technology, Tehran, Iran
Department of Bioscience and Biotechnology, Malek-Ashtar University of Technology, Tehran, Iran
Department of Bioscience and Biotechnology, Malek-Ashtar University of Technology, Tehran, Iran
Proteases are important enzymes that their role in various industries is undeniable. However, keeping enzymes stable during its activity in harsh conditions is so important. In this study, protease enzyme was immobilized on the porous silica particles and its stability in different temperatures and pHs was evaluated. First silica particles were aminated by 3-aminopropyltriethoxysilane then the protease enzyme was immobilized on the modified silica by glutaraldehyde cross-linking method and the immobilized enzyme’s activity was maintained for more than 40 days. Measuring the free subtilisin carlsberg enzyme activity and immobilized enzyme was performed according to the Lowry method. In another part, the effects of different pHs and temperatures on free and immobilized protease were evaluated. The immobilized protease activity was measured in temperature range between 25-75◦C and pH range 6.5-12. The absorption was read in 660nm. It is shown that the optimum temperature for immobilizaed enzyme is 50°C. The results showed that immobilized protease is more stable than free protease.
https://www.bmmj.org/article_21800_98cc8555446c287513e07ac415e2094c.pdf
Alkaline serine protease
Subtilisin
Silica gel
Immobilization
Cross-linking
eng
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
2016-07-01
2
1
59
64
21941
Evaluation of Oxidative Stress in Blood During Hemodialysis
Abdollah Ramzanighara
ra_qara@yahoo.com
1
Fereshteh Ezzatighadi
f.ezzati@ujiroft.ac.ir
2
Taghi Ghanbari
tg_ghanbari3@yahoo.com
3
university of jiroft
University of Jiroft
Central payam noor university
The number of patients with end-stage renal disease is growing rapidly in Asia. Patients with end stage renal disease failure (ESRD) undergoing long term hemodialysis (HD) are at risk for high oxidative stress. There is paucity of information with regard to oxidative stress during HD. Therefore, the aim of the present study was to evaluate catalase enzyme activity in erythrocytes and the total antioxidant capacity (TAC) in plasma before, during and after dialysis in hemodialysis patients. The cross-sectional study carried out in thirty four patients (16 males and 18 females) having mean age of 55 ± 16 years undergoing HD three times per week were included. The enzyme activity of catalase was measured by UV Spectrophotometric method and total antioxidant capacity in plasma were observed by ferric reducing ability of plasma (FRAP) assay method. All tests were performed before, during and after the process of dialysis. The prevalence of erythrocyte catalase enzyme activity was observed to be significantly decreased (P<0.001) during (107.01 ± 36.2) and after (105.30± 36.75) dialysis as compared to its activity before (159.75 ± 30.98) dialysis. On the other hand, a total antioxidant capacity in plasma was noticed to be significantly elevated (P<0.001) during (648.52 ± 14.66) and after (573.08 ± 15.16) dialysis as compared to before (486.61 ± 14.86) dialysis. The study concluded that dialysis process affects erythrocyte catalase enzyme activity as well as total antioxidant capacity in plasma of patients. HD exacerbates oxidative stress and disturbances in antioxidant enzymes in patients.
https://www.bmmj.org/article_21941_255525f0cf6ec98be14bafe605323954.pdf
Catalase
Total antioxidant
Hemodialysis
Oxidative stress
eng
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
2016-07-01
2
1
65
77
23116
Biophysical and Molecular Docking Studies of Human Serum Albumin Interactions with a Potential Anticancer Pt(II) Complex
Somaye Shahraki
somaye_shahraki@yahoo.com
1
Fereshteh Shiri
fereshteh.shiri@gmail.com
2
Hassan Mansouri-Torshizi
hmtorshizi@hamoon.usb.ac.ir
3
Department of Chemistry, University of Zabol, Zabol
Department of Chemistry, University of Zabol
Department of Chemistry, University of Sistan & Baluchestan, Zahedan
The interaction between [Pt(phen)(pyrr-dtc)]NO3 (where phen = 1,10-phenanthroline and pyrr-dtc =pyrrolidinedithiocarbamat) with human serum albumin (HSA) was studied by fluorescence, UV–vis absorption, circular dichroism (CD) spectroscopy and molecular docking technique under like physiological condition in Tris–HCl buffer solution at pH 7.4. UV-Vis absorption spectroscopy indicates that the protein chain was unfolded upon the addition of Pt(II) complex. Experimental results imply that the Pt(II) complex has a strong ability to quench the intrinsic fluorescence of HSA through a static quenching process. Binding constants (Kb = 2.8, 2.6 and 2.5 ×105 M-1) and the number of binding sites (n ~ 1) were calculated. According to van't Hoff equation, the thermodynamic parameters revealed that hydrophobic forces played a major role when Pt(II) complex interacted with HSA. From the qualitative analysis data of CD spectra, the binding of Pt(II) complex to HSA induced conformational changes in this protein. Finally, a molecular docking was employed for identification of the active site residues and critical interactions involved.
https://www.bmmj.org/article_23116_afbe2f5424e67c3f29916eba42bfa382.pdf
Human Serum Albumin
Anticancer agent
Molecular interactions
Multispectroscopic methods
Molecular Docking
eng
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
2016-07-01
2
1
78
85
23117
Modulation of Fourier Transform Infrared Spectra and Copper Levels by Purslane (Portulaca Oleracea) Against Liver Necrosis Induced by Copper Sulphate
Fereshteh Ezzati Ghadi
fezzatighadi@yahoo.com
1
Abdollah Ramezani Ghara
a.ramzani@ujiroft.ac.ir
2
Asiyeh Amiri
asiyehamiri@yahoo.com
3
Saeed Rezaei-Zarch
srezaei@ibb.ut.ac.ir
4
university of Jiroft
University of Jiroft
Payam-e-Noor University of Taft
Payam-e-Noor University of Taft
Copper (Cu) is an essential trace element involved in normal reproduction but its over-exposure may produce some detrimental effects. The aim of this study was to investigate the effects of purslane on copper sulfate poisoning on liver structures changes. Twenty eight wistar rats were randomly allocated to four treatment groups. Group I) Control, Group II) Copper sulfate (200 mg/kg bw were applied by gavage daily for 4 wk, Group III) Purslane (gavage 400 mg/kg bw daily for 4wk) and Group IV) Combined treatment of copper sulfate and purslane as described in Group II and III. Animals were sacrificed after four weeks and the liver were removed for atomic absorption and Fourier transform infrared spectroscopy (FTIR). A significant increase in the levels of copper and liver weight of copper-treated rats was observed which, however, got moderated significantly upon purslane treatment. The FTIR spectra of the livers of copper-treated rats revealed a significant decrease in the lipid, protein and nucleic acids contents. Treatments with purslane appreciably restored lipids levels, protein as well as nucleic acid contents in the livers of copper-treated rats. The present study suggested that purslane have promising strategy to protect tissue from oxidative stress.
https://www.bmmj.org/article_23117_4e5547dfcd6babd65accc96aebe51618.pdf
purslane
FT-IR Spectra
Copper level
Liver necrosis
copper sulphate
eng
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
2016-07-01
2
1
86
92
23121
Structural and Activity Comparison of Native, Apo and Reconstituted Tyrosinase
Saeed Emami
sayid.emami@gmail.com
1
Mohammad-Hossein Esmaeili
esmail66@yahoo.com
2
Nematollah Gheibi
gheibi_n@yahoo.com
3
Department of Biology, Faculty of Basic Sciences, Islamic Azad University Science and Research Branch, Tehran, Iran
Cellular and Molecular Research Center, Qazvin University of Medical Sciences, Qazvin, Iran
Cellular and Molecular Research Center, Qazvin University of Medical Sciences, Qazvin, Iran
Background: Mushroom Tyrosinase a potent candidate in clinical studies known as polyphenol oxidase, is a metaloenzyme from the oxidase superfamily widely distributed from lower to higher life forms. It plays a crucial role in sclerotization of exoskeleton in insects, also responsible for skin pigmentation in mammalians. Objective: In this study, after reconstitution of MT by some metal ions, the activity and structure of native, apo and reconstituted enzymes were investigated. Materials and Methods: Kinetic of reconstituted tyrosinase carried out in catecholase reaction by depletion of caffeic acid. Tertiary and secondary structure of apo, native and metal reconstituted Tyrosinase obtained with fluorescence and circular dichroism techniques respectively. Reconstitution confirmed by Atomic Absorption Spectroscopy. Results: kinetic assessment showed higher activity of MT reconstituted by Cu2+ and Ni2+ in comparison with native, Zn2+ and Co2+ reconstituted enzyme. The tertiary structure of enzyme by fluorescence technique indicated more stability of Ni2+ reconstituted MT and the apo form showed the lowest tertiary structure. Circular dichroism study showed that Ni2+ reconstituted MT form has more regular secondary structure and it caused higher stability of the enzyme. The molar ratio values from atomic absorption indicate that Ni2+ and Cu2+ have got the most binding to the apoenzyme. Conclusions: It has been shown that Ni2+, Zn2+ and Co2+ can replace Cu2+ in tyrosinase, indicating that the histidines at the active site of the tyrosinase family enzymes can reconstitute with this metals, but, the most stabilization and well-structured enzyme was observed in the apotyrosinase reconstituted by Ni+2.
https://www.bmmj.org/article_23121_1f453421ca15d180b0f78f738e468758.pdf
Tyrosinase
Reconstitution
Activity
Protein structure
Metal ions