title: ÐÑÑÐ»ÐµÐ´Ð¾Ð²Ð°Ð½Ð¸Ðµ Ð²ÑÐµÐ¼Ñ-ÑÐ°Ð·ÑÐµÑÐµÐ½Ð½Ð¾Ð¹ ÑÐ»ÑÐ¾ÑÐµÑÑÐµÐ½ÑÐ¸Ð¸ NADPH Ð¿ÑÐ¸ ÑÐ²ÑÐ·ÑÐ²Ð°Ð½Ð¸Ð¸ Ñ ÑÐµÑÐ¼ÐµÐ½ÑÐ°Ð¼Ð¸ Ð¼ÐµÑÐ¾Ð´Ð¾Ð¼ ÑÐ»ÑÐ¾ÑÐµÑÑÐµÐ½ÑÐ½Ð¾Ð¹ Ð²ÑÐµÐ¼Ñ-ÑÐ°Ð·ÑÐµÑÐµÐ½Ð½Ð¾Ð¹ Ð»Ð°Ð·ÐµÑÐ½Ð¾Ð¹ ÑÐ¿ÐµÐºÑÑÐ¾ÑÐºÐ¾Ð¿Ð¸Ð¸
title: Ð²ÑÐ¿ÑÑÐºÐ½Ð°Ñ ÐºÐ²Ð°Ð»Ð¸ÑÐ¸ÐºÐ°ÑÐ¸Ð¾Ð½Ð½Ð°Ñ ÑÐ°Ð±Ð¾ÑÐ° Ð±Ð°ÐºÐ°Ð»Ð°Ð²ÑÐ°
titleType: Subtitle
title: Research of the fluorescence decay of NADPH molecules upon binding to enzymes using polarization fluorescence laser spectroscopy
Creators: name: ÐÑÑÑÑÐºÐ¾, ÐÐ²Ð°-ÐÐ°ÑÐµÑÐ¸Ð½Ð°
Publisher: name: Ð¡Ð°Ð½ÐºÑ-ÐÐµÑÐµÑÐ±ÑÑÐ³ÑÐºÐ¸Ð¹ Ð¿Ð¾Ð»Ð¸ÑÐµÑÐ½Ð¸ÑÐµÑÐºÐ¸Ð¹ ÑÐ½Ð¸Ð²ÐµÑÑÐ¸ÑÐµÑ ÐÐµÑÑÐ° ÐÐµÐ»Ð¸ÐºÐ¾Ð³Ð¾
Year: 2024
Subjects: ÑÐ»ÑÐ¾ÑÐµÑÑÐµÐ½ÑÐ¸Ñ
Ð²ÑÐµÐ¼Ñ-ÑÐ°Ð·ÑÐµÑÐµÐ½Ð½Ð°Ñ ÑÐ»ÑÐ¾ÑÐµÑÑÐµÐ½ÑÐ½Ð°Ñ Ð´Ð²ÑÑ ÑÐ¾ÑÐ¾Ð½Ð½Ð¾Ðµ Ð²Ð¾Ð·Ð±ÑÐ¶Ð´ÐµÐ½Ð¸Ðµ
Ð°Ð½Ð¸Ð·Ð¾ÑÑÐ¾Ð¿Ð¸Ñ ÑÐ»ÑÐ¾ÑÐµÑÑÐµÐ½ÑÐ¸Ð¸
Ð±Ð¸Ð¾Ð¼Ð¾Ð»ÐµÐºÑÐ»Ñ
ÐºÐ¾ÑÐµÑÐ¼ÐµÐ½ÑÑ
ÑÐ¿ÐµÐºÑÑÐ¾ÑÐºÐ¾Ð¿Ð¸Ñ
Ð¿Ð¾Ð»ÑÑÐ¸Ð·Ð°ÑÐ¸Ñ ÑÐ»ÑÐ¾ÑÐµÑÑÐµÐ½ÑÐ¸Ð¸
fluorescence
fluorescence lifetime spectroscopy
two-photon excitation
fluorescence anisotropy
biomolecules
coenzymes
fluorescence polarization

description: ÐÐ°Ð½Ð½Ð°Ñ ÑÐ°Ð±Ð¾ÑÐ° Ð¿Ð¾ÑÐ²ÑÑÐµÐ½Ð° Ð¸ÑÑÐ»ÐµÐ´Ð¾Ð²Ð°Ð½Ð¸Ñ Ð·Ð°ÑÑÑÐ°Ð½Ð¸Ñ Ð¿Ð¾Ð»ÑÑÐ¸Ð·Ð¾Ð²Ð°Ð½Ð½Ð¾Ð¹ ÑÐ»ÑÐ¾ÑÐµÑÑÐµÐ½ÑÐ¸Ð¸ NADPH Ð² ÑÐ²Ð¾Ð±Ð¾Ð´Ð½Ð¾Ð¹ ÑÐ¾ÑÐ¼Ðµ Ð¸ ÑÐ²ÑÐ·Ð°Ð½Ð½Ð¾Ð³Ð¾ Ñ ÑÐµÑÐ¼ÐµÐ½ÑÐ°Ð¼Ð¸ IDH Ð¸ ADH. Ð Ð½Ð°ÑÑÐ¾ÑÑÐµÐµ Ð²ÑÐµÐ¼Ñ ÑÐ°ÑÐ¿ÑÐ¾ÑÑÑÐ°Ð½ÐµÐ½Ð½ÑÐ¼ Ð¼ÐµÑÐ¾Ð´Ð¾Ð¼ Ð¸ÑÑÐ»ÐµÐ´Ð¾Ð²Ð°Ð½Ð¸Ñ Ð¿ÑÐ¾ÑÐµÑÑÐ¾Ð² ÑÐµÐ»Ð°ÐºÑÐ°ÑÐ¸Ð¸, Ð¿ÑÐ¾ÑÐµÐºÐ°ÑÑÐ¸Ñ Ð² Ð²Ð¾Ð·Ð±ÑÐ¶Ð´ÐµÐ½Ð½ÑÑ Ð±Ð¸Ð¾Ð¼Ð¾Ð»ÐµÐºÑÐ»Ð°Ñ, ÑÐ²Ð»ÑÐµÑÑÑ Ð²ÑÐµÐ¼Ñ-ÑÐ°Ð·ÑÐµÑÐµÐ½Ð½Ð°Ñ ÑÐ»ÑÐ¾ÑÐµÑÑÐµÐ½ÑÐ½Ð°Ñ ÑÐ¿ÐµÐºÑÑÐ¾ÑÐºÐ¾Ð¿Ð¸Ñ. ÐÐ»Ð°Ð³Ð¾Ð´Ð°ÑÑ ÑÐ¿ÐµÐºÑÑÐ°Ð»ÑÐ½ÑÐ¼ Ð¾ÑÐ¾Ð±ÐµÐ½Ð½Ð¾ÑÑÑÐ¼ NADPH Ð¸ÑÐ¿Ð¾Ð»ÑÐ·ÑÐµÑÑÑ Ð´Ð»Ñ Ð½ÐµÐ¸Ð½Ð²Ð°Ð·Ð¸Ð²Ð½Ð¾Ð¹ Ð´Ð¸Ð°Ð³Ð½Ð¾ÑÑÐ¸ÐºÐ¸ Ð¼ÐµÑÐ°Ð±Ð¾Ð»Ð¸Ð·Ð¼Ð° ÐºÐ»ÐµÑÐ¾Ðº ÐºÐ°Ðº ÑÐ»ÑÐ¾ÑÐµÑÑÐµÐ½ÑÐ½ÑÐ¹ Ð²Ð½ÑÑÑÐ¸ÐºÐ»ÐµÑÐ¾ÑÐ½ÑÐ¹ Ð¼Ð°ÑÐºÐµÑ. Ð¦ÐµÐ»ÑÑ ÑÐ°Ð±Ð¾ÑÑ ÑÐ²Ð»ÑÐ»Ð¾ÑÑ Ð¸ÑÑÐ»ÐµÐ´Ð¾Ð²Ð°Ð½Ð¸Ðµ Ð¸ Ð°Ð½Ð°Ð»Ð¸Ð· Ð¼ÐµÑÐ°Ð½Ð¸Ð·Ð¼Ð¾Ð² ÑÐµÐ»Ð°ÐºÑÐ°ÑÐ¸Ð¸ Ð²Ð¾Ð·Ð±ÑÐ¶Ð´ÐµÐ½Ð½Ð¾Ð³Ð¾ ÑÐ¾ÑÑÐ¾ÑÐ½Ð¸Ñ ÐºÐ¾ÑÐµÑÐ¼ÐµÐ½ÑÐ° NADPH Ð² ÑÐ°ÑÑÐ²Ð¾ÑÐµ Ð² ÑÐ²Ð¾Ð±Ð¾Ð´Ð½Ð¾Ð¹ ÑÐ¾ÑÐ¼Ðµ Ð¸ Ð² ÑÐ²ÑÐ·Ð°Ð½Ð½Ð¾Ð¹ Ñ ÑÐµÑÐ¼ÐµÐ½ÑÐ°Ð¼Ð¸ Ñ Ð¿Ð¾Ð¼Ð¾ÑÑÑ Ð¼ÐµÑÐ¾Ð´Ð° Ð¿Ð¾Ð»ÑÑÐ¸Ð·Ð°ÑÐ¸Ð¾Ð½Ð½Ð¾Ð¹ Ð²ÑÐµÐ¼Ñ-ÑÐ°Ð·ÑÐµÑÐµÐ½Ð½Ð¾Ð¹ ÑÐ»ÑÐ¾ÑÐµÑÑÐµÐ½ÑÐ½Ð¾Ð¹ ÑÐ¿ÐµÐºÑÑÐ¾ÑÐºÐ¾Ð¿Ð¸Ð¸. ÐÐ°Ð´Ð°ÑÐ¸ Ð¸ÑÑÐ»ÐµÐ´Ð¾Ð²Ð°Ð½Ð¸Ñ: Ð¿ÑÐ¾Ð²ÐµÑÑÐ¸ Ð¸Ð·Ð¼ÐµÑÐµÐ½Ð¸Ñ ÑÐ¸Ð³Ð½Ð°Ð»Ð¾Ð² Ð·Ð°ÑÑÑÐ°Ð½Ð¸Ñ ÑÐ»ÑÐ¾ÑÐµÑÑÐµÐ½ÑÐ¸Ð¸ NADPH Ð² ÑÐ²Ð¾Ð±Ð¾Ð´Ð½Ð¾Ð¹ Ð¸ ÑÐ²ÑÐ·Ð°Ð½Ð½Ð¾Ð¹ ÑÐ¾ÑÐ¼Ðµ, Ð¾Ð±ÑÐ°Ð±Ð¾ÑÐ°ÑÑ ÑÐ¸Ð³Ð½Ð°Ð»Ñ, Ð¾Ð¿ÑÐµÐ´ÐµÐ»Ð¸ÑÑ Ð¿Ð°ÑÐ°Ð¼ÐµÑÑÑ ÑÐ»ÑÐ¾ÑÐµÑÑÐµÐ½ÑÐ¸Ð¸ Ð¸ Ð¿ÑÐ¾Ð²ÐµÑÑÐ¸ ÑÑÐ°Ð²Ð½Ð¸ÑÐµÐ»ÑÐ½ÑÐ¹ Ð°Ð½Ð°Ð»Ð¸Ð·. ÐÐ²ÑÑÑÐ¾ÑÐ¾Ð½Ð½Ð¾Ðµ Ð²Ð¾Ð·Ð±ÑÐ¶Ð´ÐµÐ½Ð¸Ðµ Ð¼Ð¾Ð»ÐµÐºÑÐ» Ð¾ÑÑÑÐµÑÑÐ²Ð»ÑÐ»Ð¾ÑÑ ÑÐµÐ¼ÑÐ¾ÑÐµÐºÑÐ½Ð´Ð½ÑÐ¼Ð¸ Ð»Ð°Ð·ÐµÑÐ½ÑÐ¼Ð¸ Ð¸Ð¼Ð¿ÑÐ»ÑÑÐ°Ð¼Ð¸ Ñ Ð´Ð»Ð¸Ð½Ð¾Ð¹ Ð²Ð¾Ð»Ð½Ñ 730-840 Ð½Ð¼. Ð ÐµÐ³Ð¸ÑÑÑÐ°ÑÐ¸Ñ Ð¿Ð¾Ð»ÑÑÐ¸Ð·Ð°ÑÐ¸Ð¾Ð½Ð½ÑÑ ÐºÐ¾Ð¼Ð¿Ð¾Ð½ÐµÐ½Ñ Ð¾ÑÑÑÐµÑÑÐ²Ð»ÑÐ»Ð°ÑÑ Ñ Ð¿Ð¾Ð¼Ð¾ÑÑÑ Ð¿ÑÐ¸Ð·Ð¼Ñ ÐÐ»Ð°Ð½Ð° Ð¸ Ð»Ð°Ð²Ð¸Ð½Ð½Ð¾Ð³Ð¾ ÑÐ¾ÑÐ¾Ð´ÐµÑÐµÐºÑÐ¾ÑÐ°. Ð Ð½Ð°ÑÑÐ¾ÑÑÐµÐ¹ ÑÐ°Ð±Ð¾ÑÐµ Ð±ÑÐ» Ð¿ÑÐ¾Ð²ÐµÐ´ÐµÐ½ Ð°Ð½Ð°Ð»Ð¸Ð· Ð¿Ð°ÑÐ°Ð¼ÐµÑÑÐ¾Ð² Ð·Ð°ÑÑÑÐ°Ð½Ð¸Ñ Ð¿Ð¾Ð»ÑÑÐ¸Ð·Ð¾Ð²Ð°Ð½Ð½Ð¾Ð¹ ÑÐ»ÑÐ¾ÑÐµÑÑÐµÐ½ÑÐ¸Ð¸ NADPH Ð² ÑÐ²Ð¾Ð±Ð¾Ð´Ð½Ð¾Ð¼ ÑÐ¾ÑÑÐ¾ÑÐ½Ð¸Ð¸ Ð¸ Ð² ÑÐ²ÑÐ·Ð°Ð½Ð½Ð¾Ð¼ Ñ ÑÐµÑÐ¼ÐµÐ½ÑÐ°Ð¼Ð¸ Ð°Ð»ÐºÐ¾Ð³Ð¾Ð»Ñ-Ð´ÐµÐ³Ð¸Ð´ÑÐ¾Ð³ÐµÐ½Ð°Ð·Ð¾Ð¹ (ADH) Ð¸ Ð¸Ð·Ð¾ÑÐ¸ÑÑÐ°Ñ-Ð´ÐµÐ³Ð¸Ð´ÑÐ¾Ð³ÐµÐ½Ð°Ð·Ð¾Ð¹ (IDH). ÐÐ¾Ð»ÑÑÐµÐ½Ð½ÑÐ¹ ÑÐµÐ·ÑÐ»ÑÑÐ°Ñ Ð¼Ð¾Ð¶ÐµÑ Ð±ÑÑÑ Ð¸ÑÐ¿Ð¾Ð»ÑÐ·Ð¾Ð²Ð°Ð½ Ð´Ð»Ñ ÑÐ°Ð·Ð´ÐµÐ»ÐµÐ½Ð¸Ñ NADPH Ñ Ð´ÑÑÐ³Ð¸Ð¼Ð¸ ÑÐµÑÐ¼ÐµÐ½ÑÐ°Ð¼Ð¸ Ð² ÑÐ°ÑÑÐ²Ð¾ÑÐ°Ñ Ð¸ Ð¶Ð¸Ð²ÑÑ ÐºÐ»ÐµÑÐºÐ°Ñ.
description: The given work is devoted to the research of polarized fluorescence decay of NADPH in free form and bound with the enzymes IDH and ADH. Currently, a common method for researching relaxation processes occurring in excited biomolecules is fluorescence lifetime spectroscopy. Due to its spectral properties, NADPH is used for non-invasive diagnosis of pendulum cells as a fluorescent intracellular marker. The purpose of the work was to study and analyze the relaxation parameters of the excited state of the coenzyme NADPH in free form and bound to enzymes using methodological polarization fluorescence lifetime spectroscopy. Research problems: to measure fluorescence decay signals of NADPH in free and bound forms, process the signals, determine fluorescence parameters, analyze and compare the results. Two-photon excitation of molecules was carried out by femtosecond laser pulses in the wavelength range 730-840 nm. Polarization components were detected using a Glan prism and an APD. In this work, we analyzed parameters of polarized fluorescence decay of NADPH in the free form and bound with the enzymes alcohol dehydrogenase (ADH) and isocitrate dehydrogenase (IDH). The result obtained can be used to separate NADPH by other coenzymes in solutions and living cells.