Optical properties of detonation nanodiamond complexes with globular proteins in water solution

It has been studied the changing of spectral characteristics of water-soluble 10 nm detonation nanodiamonds (DND) upon their complexation with a globular blood protein: bovine hemoglobin (Hb), human serum albumin (HSA) and rabbit immunoglobulin G (IgG) by fluorescence and absorption spectroscopy. The structure of the protein globule and its concentration in aqueous solution can significantly affect the complexation with DND (2·10-3 g/l) in the process of ultrasonic treatment (42 kHz). In all cases, it was observed when adding the DND the increasing of intensity of own luminescence of proteins (em = 330-346 nm) and bathochromic shift of protein luminescence bands. The magnitude of the shift of the maximum of protein luminescence bands at a protein concentration of 10-11 M was 5, 16, 18 nm, at the concentration 10-5 M - 7, 9, 2 nm for Hb, HSA and IgG, respectively. The aggregates’ size of DND was evaluated by AFM method in monocomponent film on the glass substrate. The results are of interest for investigations of the dynamic interaction of DND with biomacromolecules in vivo. © 2018 TANGER Ltd. All Rights Reserved.

Authors
Butusov L. 1, 2 , Nagovitsyn I.2, 3, 4 , Shulga A. 1 , Chudinova G.2, 4 , Vlasov I.2, 4 , Hairullina I. 1 , Kurilkin V. 1 , Kochneva M. 1
Publisher
TANGER Ltd.
Language
English
Pages
495-498
Status
Published
Volume
2017-October
Year
2018
Organizations
  • 1 RUDN University (People’s Friendship University of Russia), Moscow, Russian Federation
  • 2 Natural Science Center of General Physics Institute RAS, Moscow, Russian Federation
  • 3 Semenov Institute of Chemical Physics RAS, Moscow, Russian Federation
  • 4 National Research Nuclear University MEPhI (Moscow Engineering Physics Institute), Moscow, Russian Federation
Keywords
Albumin; Detonation nanodiamonds; Hemoglobin; Immunoglobulin G; Luminescence
Date of creation
19.10.2018
Date of change
19.10.2018
Short link
https://repository.rudn.ru/en/records/article/record/7302/
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