Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
5
2
2019
12
01
Effect of L-Arginine Modified Magnetic Nanoparticles (RMNPs) on Lysozyme in the Presence or Absence of Urea
83
94
EN
Faezeh
Kashanian
School of Biology, College of Science, University of Tehran, Tehran, Iran
kashanian@ut.ac.ir
Mehran
Habibi-Rezaei
School of Biology, College of Science, University of Tehran, Tehran, Iran. Nano-Biomedicine Center of Excellence, Nanoscience and Nanotechnology Research Center, University of Tehran, Tehran, Iran
cInstitute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
mhabibi@ut.ac.ir
Ali Akbar
Moosavi-Movahedi
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran. Center of Excellence in Biothermodynamics, University of Tehran, Tehran, Iran
moosavi@ut.ac.ir
Alireza
Bagherpour
Institute of Advanced Magnetic Materials, School of Metallurgy and Materials Engineering, College of Engineering, University of Tehran, Tehran, Iran
ali.bagherpour@alumni.ut.ac.ir
Maryam
Vatani
BioMEMs and Bioinspired Microfluidic laboratory, Biomedical Engineering Graduate Program, University of Calgary, Calgary, AB, Canada.
mvatani@mun.ca
L-Arginine (Arg or R) is a non-toxigenic, metabolically versatile and conditionally essential amino acid. Single-pot synthesis of Arg modified magnetic nanoparticles (RMNPs) was achieved using magnetite nanoparticles (MNPs) and binary function of Arg as a functional group and an alkali precipitator. This modification is supposed to offer several advantages to the MNPs from a bio-application viewpoint. Here, the influence of RMNPs in the structure and function of the model protein hen egg white lysozyme (HEWL) is reported. After synthesis of RMNPs, VSM, XRD, FT-IR, Zetasizer, TEM, and SEM were used to characterize the nanoparticles. The impact of RMNPs was investigated on lysozyme structure and activity during storage and in the processes of denaturation and refolding by dilution or dialysis using fluorescence, circular dichroism (CD) and UV/Vis spectroscopies. RMNPs revealed structural ordering or disordering effects on lysozyme in a RMNP:HEWL ratio dependent manner. Accordingly, a concentration ratio of threshold (CRT) was determined at 0.296. At ratios lower than the CRT the protein gained more ordered structure with increased helicity. Inversely, HEWL was increasingly unfolded and helicity was decreased at ratios higher than the CRT, rendering the protein more disordered after interaction with RMNPs. At RMNPs:HEWL concentration ratios above and even below the CRT, 6 M urea had a further disordering effect. Nevertheless, significant improvements were observed in the refolding of the protein due to dilution or dialysis, by courtesy of the RMNPs. The presented data helps to expand the thriving applications of RMNPs in biotechnology and biomedicine.
L-Arginine modified magnetic nanoparticle (RMNP),Hen egg white lysozyme (HEWL),stability,Denaturation,Refolding,Concentration ratio of threshold (CRT)
https://www.bmmj.org/article_40281.html
https://www.bmmj.org/article_40281_0f6eb25c51bc7e3676505ca18768a3e8.pdf
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
5
2
2019
12
01
The Effects of Apoptosis and the Cell Cycle Arresting of Valproate and Nicotinamide on U87 Cell Line
95
104
EN
Hanieh
Jafary
Department of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran
h-jafary@srbiau.ac.ir
Masoud
Soleimani*
Department of Hematology, Faculty of Medical Science, Tarbiat Modares University, Tehran, Iran. Department of Stem Cell Biology, Stem Cell Technology Research Center, Tehran, Iran
soleim_m@modares.ac.ir
Abstract:<br /> Epigenetic changes such as histone acetylation changes affecting genes play an important role in the development of various human cancers. HDAC inhibitors are now approved by the FDA for the treatment of cancer malignancies as well as clinical trials for tumors. Histone deacetylases play a role in the onset and progression of many cancers through effects on cell cycle, epithelial differentiation and apoptosis. We examined the antiproliferative effects of valproate with a combination of nicotinamide in human glioblastoma U87 cell line. The MTT assay showed that valproate at 0.5 mM, when used alone weakly, suppressed proliferation of cells (39%±3.05) and combination treatment of valproate + nicotinamide strongly suppressed cell proliferation (60%±3.5). Flow cytometric analysis showed that in the treatment of cells when the combination of valproate and nicotinamide was used, it showed more inhibitory effects on cell viability than when valproate alone was used. Also, western blot analyses have done to study the acetyl-histone H3 levels, and quantitative Real time PCR were performed on expression of p21 gene in U87 cell line. The combination treatment of valproate + nicotinamide enhanced the expression of p21 gene. The biological response of the cell line correlated with the increase of histone H3 acetylation after nicotinamide and valproate application. The findings indicate that co-administration of valproate and nicotinamide can have inhibitory effects on the growth and proliferation of human glioblastoma U-87 cells and may be a suitable option for new treatments for brain tumors.<br /> Key words: U87 cell, HDAC, HAT, Valproate, Nicotinamide
U87 cell,HDAC,HAT,Valproate,Nicotinamide
https://www.bmmj.org/article_40290.html
https://www.bmmj.org/article_40290_2d39fef476ef0ed357d350f8550fa726.pdf
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
5
2
2019
12
01
A Nanocarrier Based on Protein and Reduced Graphene Oxide for Sustained Release and Improvement of Carboplatin Efficacy in Cancer Treatment
105
112
EN
Jaber
Khodadi
Department of Nanotechnology and Advanced Materials, Materials and Energy Research Center, Karaj, Iran
jaber.khodadi@gmail.com
Maryam
Saeidifar
Department of Nanotechnology and Advanced Materials, Materials and Energy Research Center, Karaj, Iran
m.saidifar@gmail.com
Mona
Shahlaei
Department of Nanotechnology and Advanced Materials, Materials and Energy Research Center, Karaj, Iran
munashahlaei@yahoo.com
Adeleh
Divsalar
Department of Biological Sciences, Kharazmi University, Tehran, Iran
divsalar@khu.ac.ir
Parvaneh
Sangpour
Department of Nanotechnology and Advanced Materials, Materials and Energy Research Center, Karaj, Iran
saeidifar@merc.ac.ir
Nano-drug delivery has attracted great attention in improving the efficacy of anticancer drugs. This study described the preparation of a nanosize carrier based on protein and reduced graphene oxide (rGO) for sustained release and the enhancement of the treatment efficacy of carboplatin in breast cancer cell lines. Moreover, the characterization of bovine serum albumin nanoparticles (BSANP)-coated rGO nanosheets (rGO-BSANP) was performed by FTIR, DLS and SEM techniques. The results demonstrated that BSANP and rGO bond to each other with an average size of 753.1 nm and a surface charge of -16.0 mV. Entrapment efficiency and drug loading of rGO-BSANP in three different ratios (1:1, 1:5 and 1:10) were determined. In vitro carboplatin release from rGO, BSANP and different ratios of rGO-BSANP at 300 min showed that the rGO-BSANP nanocarrier with 1:1 ratio was an appropriate system. Furthermore, the cytotoxicity of carboplatin, rGO-BSANP and carboplatin loaded rGO-BSANP (car@rGO-BSANP) was evaluated using the MTT assay, on breast cancer cell lines, MCF7. Results showed that the presence of nanocarrier caused IC50 of carboplatin significantly decreased. Hence, the designed nanocarrier helps sustained release and a lower concentration of carboplatin for cancer treatment.
BSA nanoparticle,rGO,Release,Carboplatin,Mechanism
https://www.bmmj.org/article_43335.html
https://www.bmmj.org/article_43335_3e8bab2c06327348c2446d6adf38b59a.pdf
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
5
2
2019
12
01
Investigation of Diuron Effect as an Environmental Pollution on the Structure and Stability of Human Hemoglobin
113
128
EN
Ali
Khatibi
ORCID.0000-0003-1774-3161
Department of biotechnology, Faculty of biological sciences, Alzahra university, Tehran. Iran
khatibi@alzahra.ac.ir
Susan
Hussainzada
Department of biotechnology, Faculty of biological sciences, Alzahra university, Tehran. Iran
s.hussainzada@student.alzahra.ac.ir
Masoumeh
Heydari
Department of biotechnology, Faculty of biological sciences, Alzahra university, Tehran. Iran
heydarimasoumeh70@gmail.com
Raziyeh
Gharib
Department of biotechnology, Faculty of biological sciences, Alzahra university, Tehran. Iran
raziyeh.gharib66@gmail.com
Zahra
Moosavinejad
Department of biotechnology, Faculty of biological sciences, Alzahra university, Tehran. Iran
z.moosavinejad@alzahra.ac.ir
Abstract <br /> Diuron is being used as an herbicide in agricultural crops and non-crops areas such as roads, garden paths, and railway lines. According to clinical studies, it is slightly toxic to mammals, birds and human health. In this study, the intermolecular interaction of Diuron and human hemoglobin was investigated using various spectroscopic methods. The UV-visible and fluorescence results showed that the Diuron binds to Hb. According to the linear S-V plot, dynamic enhancement constant reduced with rising of temperature. Diuron formed a complex with HHb by static mechanism of enhancement and changed the conformation of Hb. The thermodynamic result suggested that the binding reaction was spontaneous and exothermic. Also, the result of synchronous fluorescence, heme degradation, thermal denaturation, aggregation and determination of surface hydrophobicity indicated that the Diuron could induce the conformational alteration, unfolding and heme degradation of Hb. bioanformatics study used for deciphering the binding location of a ligand to a biomicromolecules. According to molecular docking results the Diuron binds near the hydrophobic pocket of Hb which hydrophobic residue was located in this region.
Diuron,herbicide,Human hemoglobin,Stability of protein,spectroscopy
https://www.bmmj.org/article_43359.html
https://www.bmmj.org/article_43359_c84961eeb488a8fc7d2695906076b4c4.pdf
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
5
2
2019
12
01
Lack of Antioxidant Effect of Selenium on Interaction of Methyl Tert-butyl Ether (MTBE) with Cytochrome c
129
139
EN
Azin
Momen
Department of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran
momenazin@gmail.com
Masoumeh
Valipour
Department of Biology, Faculty of Science, Azarbaijan Shahid Madani University, Tabriz, Iran
valipour65@alumni.ut.ac.ir
Parvaneh
Maghami
Department of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran
maghami@srbiau.ac.ir
Shohreh
Ariaeenejad
Department of Systems and Synthetic Biology, Agricultural Biotechnology Research Institute of Iran (ABRII), Agricultural Research Education and Extension Organization (AREO), Karaj, Iran
shariaee@gmail.com
Antioxidants are of great importance because they can protect the body from oxidation agents. Reactive oxygen species (ROS) are constantly producing as a result of metabolic processes. However, environmental factors such as methyl tert-butyl ether (MTBE) can enhance oxidation stress. MTBE is a widely used fuel oxygenation liquid that has been shown to cause potential cancer. The use of antioxidants may help to reduce the oxidation condition caused by MTBE. Selenium is an essential element with antioxidant property. In this study, the interaction between Cyt C and MTBE has been investigated in the absence and presence of Se. Molecular level examinations are extremely important to investigate the structural change of proteins by MTBE. In this research, molecular behaviour of Cyt c as an important model of protein, in the presence and absence of MTBE and Se is detected by biophysical methods such as UV-vis, fluorescence and FTIR spectroscopy, chemiluminescence and molecular docking. The results showed that MTBE is able to alter Cyt c tertiary structure by ROS production with no change in secondary structure and Se could not protect the protein from structural perturbation. Molecular docking was also confirmed by the prominent interaction of Cyt c with MTBE and Se at a different site. Then Se can cause the structural change of Cyt c.
Selenium,Reactive Oxygen Species,antioxidants,cytochrome c,methyl tert-butyl ether
https://www.bmmj.org/article_44261.html
https://www.bmmj.org/article_44261_3575fd1e457fc146190c87cf70cef78e.pdf
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
5
2
2019
12
01
Spectroscopic Studies on the Interaction of Gold Nanoparticles with Lysozyme
140
151
EN
Soraya
Mohammadi
Department of Biophysics, Faculty of Biological Sciences, Tarbiat Modares University, P.O. Box 14115-175,
Tehran, Iran
soraya.mohamadi@gmail.com
Khosro
Khajeh
Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, P.O. Box 14115-175, Tehran, Iran
khajehk@gmail.com
Majid
Taghdir
Department of Biophysics, Faculty of Biological Sciences, Tarbiat Modares University, P.O. Box 14115-175, Tehran, Iran;
taghdir@modares.ac.ir
Nasrin
Farahani
Department of Nanobiotechnology, Faculty of Biological Sciences, Tarbiat Modares University, P.O. Box 14115-175, Tehran, Iran
nasrinfarahani63@gmail.com
Bijan
Ranjbar
Department of Biophysics, Faculty of Biological Sciences, Tarbiat Modares University, P.O. Box 14115-175, Tehran, Iran
ranjbarb@modares.ac.ir
Gold nanoparticles are promising materials for biomedical applications because of the attractive optical properties such as the absorption and scattering of light at resonant wavelength. Due to the fruitful applications of gold nanoparticles (GNPs), they are appropriate for a variety of biological studies. One of the most important applications of nanoparticles is protein carriers, in which transport of therapeutically relevant protein is done to in vivo or in vitro targets. Protein folding and properties of probable intermediates during the folding of proteins had been investigated in several studies. The molten globule state, a main intermediate of protein folding, has native-like secondary but perturbation of tertiary structure. Consequently, the influence of gold nanoparticles concentration on a model protein was studied by far- and near-UV circular dichroism (CD), Fourier transform infrared spectroscopy (FTIR), UV-visible spectroscopy, dynamic light scattering (DLS), transmission electron microscopy (TEM), intrinsic fluorescence emission spectroscopy and 8-Anilino-1-naphthalenesulfonic acid binding. The results indicated that the interactions between gold nanoparticles and lysozyme lead to the formation of molten globule-like state.
Gold nanoparticles,Molten globule-like state,Lysozyme,Circular dichroism
https://www.bmmj.org/article_44263.html
https://www.bmmj.org/article_44263_a2f7b8999e74eb197628a5dda81aa20a.pdf
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
5
2
2019
12
01
Self-assembly of Gold Nanoparticles Using HPI S-layer Proteins Biotemplate
152
160
EN
Maryam
Abdolirad
Faculty of Chemistry and Chemical Engineering,Malek-Ashtar University of Technology, Tehran, Iran
maryamabdolirad@gmail.com
Rassoul
khalilzadeh
Faculty of Chemistry and Chemical Engineering,Malek-Ashtar University of Technology, Tehran, Iran
rkhalilzadeh@mut.ac.ir
Mahdi
Alijanianzadeh
Department of Cell & Molecular Biology, Faculty of Biological Sciences, Kharazmi, Karaj, , Iran
alijanian@ut.ac.ir
Bacterial cell-surface proteins (S-layer proteins) have an extremely repetitive surface structure well suited as a biotemplate to fabricate metallic/semiconducting nanostructures; an issue of high importance to the electronic industry. The surface layer proteins of Deinococcus radiodurans R1 (HPI) is an attractive S-layer for arraying nanoparticles. It illustrates hexagonal symmetry which is composed of a hexameric protein core unit with a middle hole. In this study, hexagonally structure of HPI protein was confirmed by AFM. Transmission electron microscopy and Fourier transform analysis revealed the formation of hexagonally ordered arrays of 4.5nm citrate-capped Au nanoparticles. Also, the influence of stability and dispersity of gold nanoparticles has been investigated on the fabrication of ordered arrays by nanoparticle’s zeta potential. The results reflect the effect of nanoparticles’ zeta potential value on the creation of their ordered arrays through HPI layer, which could be useful in using these ordered nanoarrays for fabricating bio-sensors and some electronic devices.
Self-assembly,S-layer proteins,Biotemplate,Gold nanoparticles,Zeta Potential,TEM
https://www.bmmj.org/article_44264.html
https://www.bmmj.org/article_44264_2430c6c0f341f36e76344429baa33311.pdf
Iran Society of Biophysical Chemistry (ISOBC)
Biomacromolecular Journal
7280-2423
5
2
2019
12
01
Molecular Spectroscopy and Molecular Dynamic Simulation to Study the Binding of DNA with 3-Hydroxy-2-oxindole
161
173
EN
Fatemeh
Norouzi Rostami
Department of Chemistry, Faculty of Science, Ferdowsi University of Mashhad, Mashhad, Iran
fa.norouzi.91@stu-mail.um.ac.ir
Mohammad Reza
Housaindokht
0000-0002-5428-2512
Department of Chemistry, Faculty of Science, Ferdowsi University of Mashhad, Mashhad, Iran. Research and Technology Center of Biomolecules, Ferdowsi University of Mashhad, Mashhad, Iran
housain@um.ac.ir
Razieh
Jalal
Department of Chemistry, Faculty of Science, Ferdowsi University of Mashhad, Mashhad, Iran.
Research and Technology Center of Biomolecules, Ferdowsi University of Mashhad, Mashhad, Iran
jalal@um.ac.ir
Abbas Ali
Esmailli
Department of Chemistry, Faculty of Science, Ferdowsi University of Mashhad, Mashhad, Iran
abesmaeili@um.ac.ir
Fatemeh
Janati-Fard
Research and Technology Center of Biomolecules, Ferdowsi University of Mashhad, Mashhad, Iran
janatifard@ferdowsi.um.ac.ir
< p>This study aimed to investigate the interaction between 5-(2-hydroxy-2-oxo-2,3-dihydro-1H-indol-3-yl)-1,3thiazolidine-2,4-dione (oxindole A) and DNA with and without ultrasound treatment. Absorption studies have indicated that oxindole A could bind to CT-DNA with the binding constant of 30,000 and 26,666 M-1 with and without ultrasound treatment, respectively. In the competitive fluorescence method, the displacement of 4′,6-diamidino-2-phenylindole (DAPI) as a probe bound to the groove, from the DNA groove occurred by oxindole A. Using the Stern-Volmer plot, quenching constant was calculated to be 1,411 and 2,753 M-1 with and without ultrasound, respectively. Viscometric experiments have confirmed the groove binding of oxindole A to the DNA, which is consistent with the molecular dynamic simulation. The analysis of Pi, as a measure of affinity for ligand binding, has also revealed that the DA3, DG4, DC5, DT7, DC8, and DG9 of DNA have the highest affinity toward oxindole A. In addition, the results of the cell viability assay of the DU145 cell line have demonstrated that oxindole A has cytotoxic effects.
Interaction,CT-DNA,Oxindole,spectroscopy,Ultrasound,Simulation
https://www.bmmj.org/article_44751.html
https://www.bmmj.org/article_44751_014b98aac65a327818477069f364f861.pdf