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You searched for: Author saboury Remove constraint Author: saboury Publication Year 2017 Remove constraint Publication Year: 2017
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1. The formation of non-heat-treated whey protein cold-set hydrogels via non-toxic chemical cross-linking

Author:
Saboury, Ali Akbar,   et al.   ; Abaee, Arash; Madadlou, Ashkan;     Show all 3 Authors
Source:
Food hydrocolloids 2017 v.63 pp. 43-49
ISSN:
0268-005X
Subject:
citric acid; crosslinking; gelation; histidine; hydrocolloids; hydrogels; microstructure; pH; protein aggregates; scanning electron microscopy; spectroscopy; temperature; turbidity; whey protein
Abstract:
... A new cold-set gelation method based on the cross-linking of non-heat-treated whey protein upon alkali-catalysis in the presence of citric acid and at low temperature was established in the current study. For this purpose, different concentrations of citric acid were applied to the WPI solution at various pH values (7.0–11.0), to induce protein cross-linking reaction with time. Cross-linking incre ...
DOI:
10.1016/j.foodhyd.2016.08.024

2. Conjugation of biogenic polyamine (putrescine) with proteinase K: Spectroscopic and theoretical insights

Author:
Saboury, Ali Akbar,   et al.   ; Hosseini-Koupaei, Mansoore; Shareghi, Behzad;     Show all 3 Authors
Source:
International journal of biological macromolecules 2017 v.98 pp. 150-158
ISSN:
0141-8130
Subject:
circular dichroism spectroscopy; hydrogen; industrial applications; kinetics; peptidase K; polyamines; proteins; putrescine; solvents; van der Waals forces
Abstract:
... To understand the influence of polyamine on conformation, stabilization and function of proteins, we used multispectroscopic and simulation methods through structural, stability and kinetic measurements of proteinase K (PK) as a model enzyme combined with putrescine (Put). Structural variability of PK was investigated at different concentrations of Put, using circular dichroism, spectrofluorescenc ...
DOI:
10.1016/j.ijbiomac.2017.01.111

3. Magnetic cellulose ionomer/layered double hydroxide: An efficient anion exchange platform with enhanced diclofenac adsorption property

Author:
Saboury, Ali Akbar,   et al.   ; Hossein Beyki, Mostafa; Mohammadirad, Mosleh; Shemirani, Farzaneh;     Show all 4 Authors
Source:
Carbohydrate polymers 2017 v.157 pp. 438-446
ISSN:
0144-8617
Subject:
adsorption; anion exchange; biosorption; cellulose; diclofenac; epichlorohydrins; hydroxides; iron; kinetics; magnetite; methanol; pyridines; toxicity
Abstract:
... Polymeric ionomers with anion exchange capability are considered to be classes of environmentally friendly compounds as combination of them with anionic layered hydroxides constitute emerging advance materials. Biosorption by polymeric ionomer – layered double hydroxide (LDH) hybrid material exhibits an attractive green, low cost and low toxic – clean way. As a result, a novel anion exchange platf ...
DOI:
10.1016/j.carbpol.2016.10.017

4. Molecular investigation on the interaction of spermine with proteinase K by multispectroscopic techniques and molecular simulation studies

Author:
Saboury, Ali Akbar,   et al.   ; Hosseini-Koupaei, Mansoore; Shareghi, Behzad; Davar, Fateme;     Show all 4 Authors
Source:
International journal of biological macromolecules 2017 v.94 pp. 406-414
ISSN:
0141-8130
Subject:
binding sites; catalytic activity; circular dichroism spectroscopy; enzyme activity; enzyme stability; fluorescence; hydrogen bonding; models; peptidase K; spermine; thermodynamics; van der Waals forces
Abstract:
... The alteration in structure, function and stability of proteinase K in the presence of spermine was investigated using spectroscopic methods and simulation techniques. The stability and enzyme activity of proteinase K-spermine complex were significantly enhanced as compared to that of the pure enzyme. The increase in the value of Vmax and the catalytic efficiency of Proteinase K in presence of spe ...
DOI:
10.1016/j.ijbiomac.2016.10.038

5. The status of glycation in protein aggregation

Author:
Saboury, Ali Akbar,   et al.   ; Taghavi, Fereshteh; Habibi-Rezaei, Mehran; Amani, Mojtaba; Moosavi-Movahedi, Ali Akbar;     Show all 5 Authors
Source:
International journal of biological macromolecules 2017 v.100 pp. 67-74
ISSN:
0141-8130
Subject:
amyloid; glycation; post-translational modification; toxicity
Abstract:
... Protein crucial function and flexibility directly depend on its whole structure which is determined by the native distribution of structural elements. Any disturbances in a protein architecture leads to many kind of abnormalities and intra- or extracellular accumulation of misfolded proteins which are the basis of conformational diseases. Glycation is one of the most important unwanted post-transl ...
DOI:
10.1016/j.ijbiomac.2015.12.085

6. The functional and structural stabilization of trypsin by sucrose

Author:
Saboury, Ali Akbar,   et al.   ; Momeni, Lida; Mahmodian, Sheida; Shareghi, Behzad; Farhadian, Sadegh;     Show all 5 Authors
Source:
International journal of biological macromolecules 2017 v.99 pp. 343-349
ISSN:
0141-8130
Subject:
absorption; binding sites; circular dichroism spectroscopy; enthalpy; entropy; fluorescence; fluorescence emission spectroscopy; hydrogen bonding; hydrophobicity; melting point; moieties; molecular models; protein unfolding; spectral analysis; sucrose; thermal stability; trypsin
Abstract:
... Docking and spectroscopic techniques were performed to probe the stabilizing effect of sucrose on the dynamics, structure and activity of trypsin. The thermodynamic folding properties, melting temperature (Tm), enthalpy change (ΔH°) and entropy change (ΔS°) were measured by thermal stability studies to understand the picture of trypsin folding. Sucrose acted as an enhancer for trypsin stability. F ...
DOI:
10.1016/j.ijbiomac.2017.02.090

7. A spectroscopic and thermal stability study on the interaction between putrescine and bovine trypsin

Author:
Saboury, Ali A.,   et al.   ; Momeni, Lida; Shareghi, Behzad; Farhadian, Sadegh; Reisi, Fateme;     Show all 5 Authors
Source:
International journal of biological macromolecules 2017 v.94 pp. 145-153
ISSN:
0141-8130
Subject:
absorbance; cattle; circular dichroism spectroscopy; enthalpy; entropy; fluorescence; fluorescence emission spectroscopy; hydrogen bonding; hydrophobicity; molecular models; putrescine; thermal stability; trypsin; van der Waals forces
Abstract:
... The interaction of putrescine with bovine trypsin was investigated using steady state thermal stability, intrinsic fluorescence, UV–vis spectroscopy, far and near- UV circular dichroism and kinetic techniques, as well as molecular docking. The Stern-Volmer quenching constants for the trypsin- putrescine complex were calculated revealing that putrescine interacted with trypsin via the static fluore ...
DOI:
10.1016/j.ijbiomac.2016.10.009

8. Generation of reactive oxygen species via inhibition of liver catalase by oxalli-palladium: A spectroscopic and docking study

Author:
Saboury, Ali Akbar,   et al.   ; Gholamian, Azam; Divsalar, Adeleh; Saiedifar, Maryam; Ghalandari, Behafarid; Koohshekan, Bahare;     Show all 6 Authors
Source:
Process biochemistry 2017 v.52 pp. 165-173
ISSN:
1359-5113
Subject:
adverse effects; antineoplastic activity; antineoplastic agents; binding sites; catalase; cattle; circular dichroism spectroscopy; electrostatic interactions; emissions factor; enzyme inhibition; fluorescence; fluorescence emission spectroscopy; liver; molecular models; reactive oxygen species
Abstract:
... In the present study, the side effects of an anti-cancer compound of oxali-palladium on the function and structure of bovine liver catalase (BLC) were investigated using multiple spectroscopic (fluorescence, circular dichroism (CD) and UV–vis) and molecular docking methods. Results of kinetics study showed a noncompetitive inhibition of the enzyme for oxali-palladium. Addition of various concentra ...
DOI:
10.1016/j.procbio.2016.10.012

9. Red/ox states of human protein disulfide isomerase regulates binding affinity of 17-Beta-Estradiol

Author:
Saboury, Ali Akbar,   et al.   ; Karamzadeh, Razieh; Karimi-Jafari, Mohammad Hossein; Hosseini-Salekdeh, Ghasem; Moosavi-Movahedi, Ali Akbar;     Show all 5 Authors
Source:
Archives of biochemistry and biophysics 2017
ISSN:
0003-9861
Subject:
binding capacity; endoplasmic reticulum; humans; molecular chaperones; oxidation; protein disulfide-isomerase; steroid hormones
Abstract:
... Human protein disulfide isomerase (hPDI) is a key redox-regulated thiol-containing protein operating as both oxidoreductase and molecular chaperone in the endoplasmic reticulum of cells. hPDI thiol-disulfide interchange reactions lead to the adoption of two distinct red/ox conformations with different substrate preferences. hPDI also displays high binding capacity for some exogenous steroid hormon ...
DOI:
10.1016/j.abb.2017.02.010

10. The Functional and Structural Stabilization of TrypsinbySucrose

Author:
Saboury, Ali Akbar,   et al.   ; Momeni, Lida; Mahmodian, Sheida; Shareghi, Behzad; Farhadian, Sadegh;     Show all 5 Authors
Source:
International journal of biological macromolecules 2017
ISSN:
0141-8130
Subject:
absorption; binding sites; circular dichroism spectroscopy; enthalpy; entropy; fluorescence; fluorescence emission spectroscopy; hydrogen bonding; hydrophobicity; melting point; molecular models; protein unfolding; spectral analysis; sucrose; thermal stability; trypsin
Abstract:
... Docking and spectroscopic techniques were performed to probe the stabilizing effect of sucrose on the dynamics, structure and activity of trypsin. The thermodynamic folding properties, melting temperature (Tm), enthalpy change (ΔH°) and entropy change (ΔS°) were measuredby thermal stability studies to understand the picture of trypsin folding. Sucrose acted as an enhancer for trypsin stability. Fl ...
DOI:
10.1016/j.ijbiomac.2017.02.090

11. A spectroscopic study on the absorption of carbonic anhydrase onto the nanoporous silica nanoparticle

Author:
Saboury, Ali Akbar,   et al.   ; Khameneh, Hannaneh Pourjabbari; Bolouri, Termeh Ghorbanian; Nemati, Fahimeh; Rezvani, Fatemeh; Attar, Farnoosh; Falahati, Mojtaba;     Show all 7 Authors
Source:
International journal of biological macromolecules 2017
ISSN:
0141-8130
Subject:
absorption; carbonate dehydratase; cattle; circular dichroism spectroscopy; denaturation; enzyme stability; fluorescence emission spectroscopy; hydrodynamics; immobilized enzymes; industrial applications; light scattering; melting point; nanoparticles; nanopores; pH; silica; spectral analysis; urea; zeta potential
Abstract:
... Herein, KIT-6 nanoporous silica nanoparticles were used as a solid support for immobilization of bovine carbonic anhydrase, isoform II (BCA II). The zeta potential study revealed that KIT-6 and BCA II provided negative (-13.58±1.95mV) and positive (4.23±0.72mV) charge distribution, respectively. Dynamic light scattering (DLS) analysis also showed that the hydrodynamic radius of KIT-6 is less than ...
DOI:
10.1016/j.ijbiomac.2017.03.030

12. Histidine substitution in the most flexible fragments of firefly luciferase modifies its thermal stability

Author:
Saboury, Ali Akbar,   et al.   ; Rahban, Mahdie; Salehi, Najmeh; Hosseinkhani, Saman; Karimi-Jafari, Mohammad Hossein; Firouzi, Rohoullah; Rezaei-Ghaleh, Nasrollah; Moosavi-Movahedi, Ali Akbar;     Show all 8 Authors
Source:
Archives of biochemistry and biophysics 2017 v.629 pp. 8-18
ISSN:
0003-9861
Subject:
adenosine triphosphate; aspartic acid; binding capacity; enzyme kinetics; histidine; luciferase; melting point; molecular dynamics; mutants; mutation; temperature; thermal stability
Abstract:
... Molecular dynamics (MD) at two temperatures of 300 and 340 K identified two histidine residues, His461 and His489, in the most flexible regions of firefly luciferase, a light emitting enzyme. We therefore designed four protein mutants H461D, H489K, H489D and H489M to investigate their enzyme kinetic and thermodynamic stability changes. Substitution of His461 by aspartate (H461D) decreased ATP bind ...
DOI:
10.1016/j.abb.2017.07.003

13. Selectivity of major isoquinoline alkaloids from Chelidonium majus towards telomeric G-quadruplex: A study using a transition-FRET (t-FRET) assay General subjects

Author:
Saboury, Ali A.,   et al.   ; Noureini, Sakineh Kazemi; Esmaeili, Hosein; Abachi, Farzane; Khiali, Soraia; Islam, Barira; Kuta, Martyna; Hoffmann, Marcin; Sponer, Jiri; Parkinson, Gary; Haider, Shozeb;     Show all 11 Authors
Source:
Biochimica et biophysica acta 2017 v.1861 no.8 pp. 2020-2030
ISSN:
0304-4165
Subject:
Chelidonium majus; adverse effects; antineoplastic agents; berberine; biobased products; circular dichroism spectroscopy; humans; isoquinolines; ligands; messenger RNA; molecular models; oligonucleotides; papaverine; quantitative polymerase chain reaction; sanguinarine; stabilizers; telomerase; telomeres
Abstract:
... Natural bioproducts are invaluable resources in drug discovery. Isoquinoline alkaloids of Chelidonium majus constitute a structurally diverse family of natural products that are of great interest, one of them being their selectivity for human telomeric G-quadruplex structure and telomerase inhibition.The study focuses on the mechanism of telomerase inhibition by stabilization of telomeric G-quadru ...
DOI:
10.1016/j.bbagen.2017.05.002