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полный	информационный	краткий

Поисковый запрос: (<.>S=DOCKING<.>)

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Biogenic ferrihydrite nanoparticles produced by Klebsiella oxytoca: Characterization, physicochemical properties and bovine serum albumin interactions / N. Cazacu, C. G. Chilom, S. Iftimie [et al.] // Nanomaterials. - 2022. - Vol. 12, Is. 2. - Ст. 249, DOI 10.3390/nano12020249. - Cited References: 59. - This research was funded by JINR Themes 02-1-1107-2011/2021, 04-5-1131-2017/2021 and 04-4-1133-2018/2023 and with the financial support of the RO-JINR Projects Nos. 366/11.05.2021 (items 7, 86, 97) and 365/11.05.2021 (items 8, 87 and 98). This work also benefited from the use of the SasView application, originally developed under NSF Award DMR-0520547. SasView also contains the code developed with funding from the EU Horizon 2020 program under the SINE2020 project Grant No 654000. The APC was funded by JINR Theme 02-1-1107-2011/2021, Project No. 366/11.05.2021, item 7. This study used the infrastructure of the Applied Genetics Resource Facility of MIPT (Suport Grant 075-15-2021-684) . - ISSN 2079-4991

РУБ Chemistry, Multidisciplinary + Nanoscience & Nanotechnology + Materials Science, Multidisciplinary + Physics, Applied
Рубрики:
MAGNETIC-PROPERTIES
   REDUCTION
   MOSSBAUER
   FERRITIN
   DOCKING
   BINDING
Кл.слова (ненормированные):
biogenic ferrihydrite nanoparticles -- the binding mechanism -- energy transfer -- protein stability -- molecular docking
Аннотация: The synthesis of nanoparticles inside microorganisms is an economical alternative to chemical and physical methods of nanoparticle synthesis. In this study, ferrihydrite nanoparticles synthesized by Klebsiella oxytoca bacterium in special conditions were characterized by scanning electron microscopy (SEM), energy-dispersive X-ray analysis (EDS), small-angle X-ray (SAXS), UV-Vis spectroscopy, fluorescence, fluorescence resonance energy transfer (FRET), and molecular docking. The morphology and the structure of the particles were characterized by means of SEM and SAXS. The elemental content was determined by means of the EDS method. The absorption properties of the ferrihydrite nanoparticles were investigated by UV-Vis spectroscopy. The binding mechanism of the biogenic ferrihydrite nanoparticles to Bovine Serum Albumin (BSA) protein, studied by fluorescence, showed a static and weak process, combined with FRET. Protein denaturation by temperature and urea in the presence of the ferrihydrite nanoparticles demonstrated their influence on the unfolding process. The AutoDock Vina and UCSF Chimera programs were used to predict the optimal binding site of the ferrihydrite to BSA and to find the location of the hydrophobic cavities in the sub-domain IIA of the BSA structure.

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Держатели документа:
Univ Bucharest, Fac Phys, Dept Elect Solid State & Biophys, RO-077125 Magurele, Romania.
Horia Hulubei Natl Inst Phys & Nucl Engn, Dept Nucl Phys, RO-077125 Magurele, Romania.
Joint Inst Nucl Res, Dubna 141980, Russia.
Moscow Inst Phys & Technol, Dolgoprudnyi 141701, Russia.
Russian Acad Sci, Siberian Branch, Fed Res Ctr KSC, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Sch Engn Phys & Radio Elect, Phys Dept, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Siberian Branch, Kirensky Inst Phys, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Cazacu, Nicoleta; Chilom, Claudia G.; Iftimie, Sorina; Balasoiu, Maria; Ladygina, Valentina P.; Stolyar, S. V.; Столяр, Сергей Викторович; Orelovich, Oleg L.; Kovalev, Yuriy S.; Rogachev, Andrey V.
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