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<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">zhps</journal-id><journal-title-group><journal-title xml:lang="ru">Журнал прикладной спектроскопии</journal-title><trans-title-group xml:lang="en"><trans-title>Zhurnal Prikladnoii Spektroskopii</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">0514-7506</issn><publisher><publisher-name>B. I. Stepanov Institute of Physics of the National Academy of Sciences</publisher-name></publisher></journal-meta><article-meta><article-id custom-type="elpub" pub-id-type="custom">zhps-1004</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>Статьи</subject></subj-group></article-categories><title-group><article-title>Глубинная УФ-светодиодная динамическая оптическая визуализация и флуоресцентная спектроскопия короны белка в плазмонном растворе и эффект нагрева излучением лазера в ближней ИК-области</article-title><trans-title-group xml:lang="en"><trans-title>Deep UV Led Dynamic Optical Imaging and Fluorescence Spectroscopy of the Protein Corona in a Plasmonic Solution and the Effect of Near-Infrared Laser Heating</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Khosroshahi</surname><given-names>М. Е.</given-names></name><name name-style="western" xml:lang="en"><surname>Khosroshahi</surname><given-names>M. E.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Онтарио</p></bio><bio xml:lang="en"><p>Ontario</p></bio><email xlink:type="simple">khosrom@mie.utoronto.ca</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Woll-Morison</surname><given-names>V.</given-names></name><name name-style="western" xml:lang="en"><surname>Woll-Morison</surname><given-names>V.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Онтарио</p></bio><bio xml:lang="en"><p>Ontario</p></bio><xref ref-type="aff" rid="aff-2"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>M.I.S. Electronics Inc.;&#13;
Университет Торонто</institution></aff><aff xml:lang="en"><institution>Nanobiophotonics &amp; Biomedical Research Laboratory, M.I.S. Electronics Inc.,&#13;
Richmond Hill;&#13;
Department of Mechanical and Industrial Engineering, University of Toronto</institution></aff></aff-alternatives><aff-alternatives id="aff-2"><aff xml:lang="ru"><institution>M.I.S. Electronics Inc.</institution></aff><aff xml:lang="en"><institution>Nanobiophotonics &amp; Biomedical Research Laboratory, M.I.S. Electronics Inc.,&#13;
Richmond Hill</institution></aff></aff-alternatives><pub-date pub-type="collection"><year>2022</year></pub-date><pub-date pub-type="epub"><day>23</day><month>03</month><year>2022</year></pub-date><volume>89</volume><issue>2</issue><fpage>210</fpage><lpage>220</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Khosroshahi М.Е., Woll-Morison V., 2022</copyright-statement><copyright-year>2022</copyright-year><copyright-holder xml:lang="ru">Khosroshahi М.Е., Woll-Morison V.</copyright-holder><copyright-holder xml:lang="en">Khosroshahi M.E., Woll-Morison V.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://zhps.ejournal.by/jour/article/view/1004">https://zhps.ejournal.by/jour/article/view/1004</self-uri><abstract><p>Исследовано взаимодействие светодиодного глубинного УФ-излучения (275 нм) с бычьим сывороточным альбумином (БСА), содержащим наночастицы золота (НЧЗ), с использованием динамического профилирования луча и флуоресцентной спектроскопии. Тепловое воздействие излучения диодного лазера с l = 800 нм на биоплазмонный раствор исследовано с помощью мониторинга зондирующего луча и ИК-камеры. Результаты показали последовательное нелинейное и колебательное поведение комплекса НЧЗ-БСА из-за процесса адсорбции и десорбции белка. Наблюдаемые усиление и тушение флуоресценции тирозина (Tyr) могут дать информацию о кинетике связывания и конформационных изменениях белка. После лазерного нагрева в течение 10 мин флуоресценция Tyr полностью исчезает и зондирующий пучок He–Ne расширяется на ~4 нм из-за столкновений молекул и денатурации белка. Изменение температуры вследствие разворачивания и денатурации белка демонстрирует аналогичную нелинейную картину при разных объемах НЧЗ. Однако температура ниже при более высоких концентрациях НЧЗ, что указывает на более высокую скорость адсорбции белка, способствующую уменьшению локализованного поверхностного плазмонного резонанса посредством нагревания.</p></abstract><trans-abstract xml:lang="en"><p>When plasmonic nanoparticles (PNPs) enter a biofluid, the adsorbed biomolecules on the surface form a protein corona, which has direct consequences in biomedical applications. The binding in passive adsorption is nonspecific and is governed by ionic, van der Waals, and hydrophobic forces. We describe the results of deep LED (275-nm) interaction with bovine serum albumin (BSA) containing gold nanourchin (GNU) using dynamic beam view profiling and fluorescence spectroscopy. 800-nm diode laser-induced thermal effects on the bioplasmonic solution were investigated using probe beam monitoring and an IR camera. The results indicated a consistent nonlinear and oscillatory behavior of the GNU-BSA complex due to the adsorption and desorption process of protein. Tyrosine (Tyr) fluorescence enhancement and quenching were observed, which can provide some information about the binding kinetics and protein conformational changes. After 10 min of laser heating, the Tyr fluorescence completely vanished and the He-Ne probe beam was broadened by about 4 nm owing to molecular collisions and protein denaturation. The temperature variation due to protein unfolding and denaturation exhibited a similar nonlinear pattern at different GNU volumes. However, the temperature was lower at higher GNU concentrations, indicating a higher rate of protein adsorption, which effectively mitigated the localized surface plasmon resonance heating.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>корона белка</kwd><kwd>наночастица золота</kwd><kwd>бычий сывороточный альбумин</kwd><kwd>флуоресцентная спектроскопия</kwd><kwd>оптическая визуализация</kwd><kwd>тепловой эффект</kwd></kwd-group><kwd-group xml:lang="en"><kwd>protein corona</kwd><kwd>gold nanourchin</kwd><kwd>bovine serum albumin</kwd><kwd>fluorescence spectroscopy</kwd><kwd>optical imaging</kwd><kwd>thermal effects</kwd></kwd-group><funding-group><funding-statement xml:lang="ru">The authors would like to thank and acknowledge MIS Electronics Inc. for funding the research at the Nanobiophotonics &amp; Biomedical Research Lab.</funding-statement><funding-statement xml:lang="en">The authors would like to thank and acknowledge MIS Electronics Inc. for funding the research at the Nanobiophotonics &amp; Biomedical Research Lab.</funding-statement></funding-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">J. 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