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  1. AU="Hosseinzadeh, Sara Ali"
  2. AU="Lee, Kristen"
  3. AU="Gentile, Giulia"
  4. AU="Shoben, Abigail B."
  5. AU="Rowe, Elizabeth"
  6. AU="Pandemic Response COVID-19 Research Collaboration Platform for HCQ/CQ Pooled Analyses"
  7. AU="Rahali, Anwar"
  8. AU="Zhang, Zhuang-Wei"
  9. AU="Townsend, Elizabeth C"
  10. AU="Lange, Mona V"
  11. AU="Bruner, Brenda G"
  12. AU="Michael Craigen"
  13. AU="Lambard, G."
  14. AU="Dempsey, Connor P"
  15. AU=Li Youxian
  16. AU="Bhosale, Chanakya R"

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  1. Artikel: Synthesis of Ni

    Shariati, Alireza / Hosseinzadeh, Sara Ali / Barghi, Zahra / Mortazavi, Sogand Sadat / Atarod, Kosar / Shariati, Fatemeh Sadat / Farahmand, Behrokh

    AMB Express

    2023  Band 13, Heft 1, Seite(n) 112

    Abstract: Facilitated purification of proteins, at a low cost and a short time, is one of the key steps in the industrial production of recombinant proteins. In the current study, polydopamine nanoparticles (PDA-NPs) are considered in the synthesis of magnetic ... ...

    Abstract Facilitated purification of proteins, at a low cost and a short time, is one of the key steps in the industrial production of recombinant proteins. In the current study, polydopamine nanoparticles (PDA-NPs) are considered in the synthesis of magnetic beads for purifying recombinant proteins due to advantages such as biocompatibility/ biodegradability, easy synthesis, as well as the ability to directly chelate metal ions. They were synthesized in Tris buffer (pH: 8:5), then chelated with Fe
    Sprache Englisch
    Erscheinungsdatum 2023-10-13
    Erscheinungsland Germany
    Dokumenttyp Journal Article
    ZDB-ID 2621432-5
    ISSN 2191-0855
    ISSN 2191-0855
    DOI 10.1186/s13568-023-01613-z
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Gold nanoparticle conjugation enhances berberine's antibacterial activity against methicillin-resistant Staphylococcus aureus (MRSA).

    Sadeghi, Somayeh / Agharazi, Fatemeh / Hosseinzadeh, Sara Ali / Mashayekhi, Mohammad / Saffari, Zahra / Shafiei, Morvarid / Nader Shahrokhi / Ebrahimi-Rad, Mina / Sadeghi, Mahdi

    Talanta

    2023  Band 268, Heft Pt 1, Seite(n) 125358

    Abstract: Nanoparticle (NP) conjugation with various biomolecules is one of the most promising approaches for targeting Methicillin-resistant Staphylococcus aureus (MRSA). In this study, berberine (BER) was conjugated with gold nanoparticles (AuNPs) to enhance its ...

    Abstract Nanoparticle (NP) conjugation with various biomolecules is one of the most promising approaches for targeting Methicillin-resistant Staphylococcus aureus (MRSA). In this study, berberine (BER) was conjugated with gold nanoparticles (AuNPs) to enhance its antibacterial activity against MRSA. Chemically synthesized AuNPs were characterized by UV-vis spectroscopy, size distribution and Field Emission-Scanning Electron Microscope (FE-SEM) analysis. Berberine was conjugated with AuNPs and the conjugants were characterized using UV-vis spectroscopy and Fourier Transform Infrared (FTIR). The cytotoxicity of free and conjugated BER was also investigated. Comparative studies were conducted based on the Minimum Inhibitory Concentration (MIC) and anti-biofilm activities of conjugants and free BER against MRSA isolates. To verify cell membrane disruption and intracellular imbalance following treatment exposure, reactive oxygen species (ROS) and live-dead staining experiments were performed. In vivo antibacterial efficacy of treated groups was also assessed in a BALB/c mouse-infected skin model. DLS measurement, FE-SEM, and UV-vis spectroscopy confirmed the synthesis of AuNPs with a narrow size distribution of 49.38 nm and a zeta potential of -31.9 mV. The results from UV-vis spectroscopy and FTIR provided support for the functionalization of AuNPs by BER functional groups. The In vitro antibacterial results demonstrated that the conjugated BER exhibited a lower MIC value against MRSA (109.5 μg/ml) compared to free BER (165 μg/ml). Free and conjugated BER, at their MIC concentrations, demonstrated anti-biofilm activity, resulting in biofilm eradication of 13.9 and 22.33 %, respectively. The highest level of ROS production (93 %) was associated with the conjugated BER at a concentration of 27.37 μg/ml. This finding indicates a disruption in cell membrane integrity and a reduction in bacterial viability, as demonstrated by ROS and live/dead staining assays. The cytotoxicity study on the mouse L929 fibroblast cell line revealed approximately 100 % cell viability when exposed to free or conjugated BER at their MIC concentration. This result indicates the biosafety of both of the compounds. The in vivo study in the infected skin model groups treated with conjugated and free BER revealed MRSA survival rate of 2.7 % and 26 %, respectively. These findings suggest that conjugated BER could be an effective nanoformulation candidate with a potential role in managing MRSA associated infections.
    Mesh-Begriff(e) Animals ; Mice ; Methicillin-Resistant Staphylococcus aureus ; Gold/pharmacology ; Gold/chemistry ; Berberine/pharmacology ; Reactive Oxygen Species ; Metal Nanoparticles/chemistry ; Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/chemistry ; Microbial Sensitivity Tests
    Chemische Substanzen Gold (7440-57-5) ; Berberine (0I8Y3P32UF) ; Reactive Oxygen Species ; Anti-Bacterial Agents
    Sprache Englisch
    Erscheinungsdatum 2023-10-29
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article
    ZDB-ID 1500969-5
    ISSN 1873-3573 ; 0039-9140
    ISSN (online) 1873-3573
    ISSN 0039-9140
    DOI 10.1016/j.talanta.2023.125358
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  3. Artikel ; Online: Improved anti-biofilm activity and long-lasting effects of novel serratiopeptidase immobilized on cellulose nanofibers.

    Rouhani, Maryam / Valizadeh, Vahideh / Bakhshandeh, Haleh / Hosseinzadeh, Sara Ali / Molasalehi, Sara / Atyabi, Seyed Mohammad / Norouzian, Dariush

    Applied microbiology and biotechnology

    2023  Band 107, Heft 21, Seite(n) 6487–6496

    Abstract: Today, enzymatic treatment is a progressive field in combating biofilm producing pathogens. In this regard, serratiopeptidase, a medicinally important metalloprotease, has been recently highlighted as an enzyme with proved anti-biofilm activity. In the ... ...

    Abstract Today, enzymatic treatment is a progressive field in combating biofilm producing pathogens. In this regard, serratiopeptidase, a medicinally important metalloprotease, has been recently highlighted as an enzyme with proved anti-biofilm activity. In the present study, in order to increase the long-lasting effects of the enzyme, serratiopeptidase and the novel engineered forms with enhanced anti-biofilm activity were immobilized on the surface of cellulose nanofibers (CNFs) as a natural polymer with eminent properties. For this, recombinant serratiopeptidases including the native and previously designed enzymes were produced, purified and conjugated to the CNF by chemical and physical methods. Immobilization was confirmed using different scanning and microscopic methods. The enzyme activity was assessed using casein hydrolysis test. Enzyme release analysis was performed using dialysis tube method. Anti-biofilm activity of free and immobilized enzymes has been examined on Staphylococcus aureus and Pseudomonas aeruginosa strains. Finally, cytotoxicity of enzyme-conjugated CNFs was performed by MTT assay. The casein hydrolysis results confirmed fixation of all recombinant enzymes on CNFs by chemical method; however, inadequate fixation of these enzymes was found using cold atmospheric plasma (CAP). The AFM, FTIR, and SEM analysis confirmed appropriate conjugation of enzymes on the surface of CNFs. Immobilization of enzymes on CNFs improved the anti-biofilm activity of serratiopeptidase enzymes. Interestingly, the novel engineered serratiopeptidase (T344 [8-339ss]) exhibited the highest anti-biofilm activity in both conjugated and non-conjugated forms. In conclusion, incorporation of serratiopeptidases into CNFs improves their anti-biofilm activities without baring any cytotoxicity. KEY POINTS: • Enzymes were successfully immobilized on cellulose nanofibers using chemical method. • Immobilization of enzymes on CNFs improved their anti-biofilm activity. • T344 [8-339ss] exhibited the highest anti-biofilm activity in both conjugated and non-conjugated forms.
    Mesh-Begriff(e) Cellulose/chemistry ; Nanofibers/chemistry ; Caseins ; Biofilms
    Chemische Substanzen Cellulose (9004-34-6) ; serratiopeptidase (NL053ABE4J) ; Caseins
    Sprache Englisch
    Erscheinungsdatum 2023-09-06
    Erscheinungsland Germany
    Dokumenttyp Journal Article
    ZDB-ID 392453-1
    ISSN 1432-0614 ; 0171-1741 ; 0175-7598
    ISSN (online) 1432-0614
    ISSN 0171-1741 ; 0175-7598
    DOI 10.1007/s00253-023-12734-7
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel: Hyaluronic acid production and characterization by novel Bacillus subtilis harboring truncated Hyaluronan Synthase.

    Amjad Zanjani, Fatemeh Sadat / Afrasiabi, Shadi / Norouzian, Dariush / Ahmadian, Gholamreza / Hosseinzadeh, Sara Ali / Fayazi Barjin, Alireza / Cohan, Reza Ahangari / Keramati, Malihe

    AMB Express

    2022  Band 12, Heft 1, Seite(n) 88

    Abstract: Hyaluronic Acid (HA) is a natural biopolymer that has important physiological and industrial applications due to its viscoelastic and hydrophilic characteristics. The responsible enzyme for HA production is Hyaluronan synthase (HAS). Although in vitro ... ...

    Abstract Hyaluronic Acid (HA) is a natural biopolymer that has important physiological and industrial applications due to its viscoelastic and hydrophilic characteristics. The responsible enzyme for HA production is Hyaluronan synthase (HAS). Although in vitro structure-function of intact HAS enzyme has been partly identified, there is no data on in vivo function of truncated HAS forms. In the current study, novel recombinant Bacillus subtilis strains harboring full length (RBSFA) and truncated forms of SeHAS (RBSTr4 and RBSTr3) were developed and HA production was studied in terms of titer, production rate and molecular weight (Mw). The maximum HA titer for RBSFA, RBSTr4 and RBSTr3 was 602 ± 16.6, 503 ± 19.4 and 728 ± 22.9 mg/L, respectively. Also, the HA production rate was 20.02, 15.90 and 24.42 mg/L.h
    Sprache Englisch
    Erscheinungsdatum 2022-07-12
    Erscheinungsland Germany
    Dokumenttyp Journal Article
    ZDB-ID 2621432-5
    ISSN 2191-0855
    ISSN 2191-0855
    DOI 10.1186/s13568-022-01429-3
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  5. Artikel ; Online: Novel serratiopeptidase exhibits different affinities to the substrates and inhibitors.

    Hosseinzadeh, Sara Ali / Valizadeh, Vahideh / Rouhani, Maryam / Mirkazemi, Sedigheh / Azizi, Masoumeh / Norouzian, Dariush / Ahangari Cohan, Reza

    Chemical biology & drug design

    2022  Band 100, Heft 4, Seite(n) 553–563

    Abstract: The clinical application of serratiopeptidase as an anti-biofilm and anti-inflammatory agent is restricted due to the enzyme sensitivity to the environmental conditions. In our previous study, six enzyme variants were designed by introducing different ... ...

    Abstract The clinical application of serratiopeptidase as an anti-biofilm and anti-inflammatory agent is restricted due to the enzyme sensitivity to the environmental conditions. In our previous study, six enzyme variants were designed by introducing different mutations and truncations that exhibited higher thermal stability. In the present study, the interaction pattern and affinity of variants to substrates and inhibitors were studied using molecular docking and in vitro studies. CABS-dock and Swiss-dock servers were used for substrate (Bradykinin and Substance-P) and inhibitor (Lisinopril and EDTA) docking, respectively. The interactions were analyzed using LigPlot, UCSF Chimera, and visual molecular dynamics packages. Free energy calculations were performed using PRODIGY. Finally, the native enzyme and the best variant in terms of interaction pattern and binding score were selected for in-vitro affinity analysis toward Bradykinin and EDTA using HPLC and casein hydrolysis test, respectively. Molecular docking revealed that T344 [8-339ss] variant showed a different pattern for both substrates and inhibitors in the way that none of the native active site residues were involved in the receptor binding. As revealed by in vitro studies, T344 [8-339ss] displayed the highest number of hydrogen bond formation in docking with Bradykinin and remarkable decrement in the binding affinity for EDTA. This was the first report on the design of novel serratiopeptidase with higher activity to Bradykinin and improved resistance to EDTA as an inhibitor.
    Mesh-Begriff(e) Anti-Inflammatory Agents ; Bradykinin ; Caseins ; Edetic Acid ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Lisinopril ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Peptide Hydrolases
    Chemische Substanzen Anti-Inflammatory Agents ; Caseins ; Edetic Acid (9G34HU7RV0) ; Lisinopril (E7199S1YWR) ; Peptide Hydrolases (EC 3.4.-) ; serratiopeptidase (NL053ABE4J) ; Bradykinin (S8TIM42R2W)
    Sprache Englisch
    Erscheinungsdatum 2022-07-01
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 2216600-2
    ISSN 1747-0285 ; 1747-0277
    ISSN (online) 1747-0285
    ISSN 1747-0277
    DOI 10.1111/cbdd.14105
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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