RGD Peptide–Albumin Conjugate for Endothelization of Electrospun Materials
- Авторы: Cherepanova A.1,2, Akisheva D.1, Popova T.1,3, Chelobanov B.1,3, Chesalov Y.4, Godovikova T.1,3, Karpenko A.2, Laktionov P.1,2
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Учреждения:
- Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences
- Meshalkin National Medical Research Center, Ministry of Health of the Russian Federation
- Novosibirsk State University
- Boreskov Institute of Catalysis, Federal Research Center, Siberian Branch, Russian Academy of Sciences
- Выпуск: Том 45, № 6 (2019)
- Страницы: 793-802
- Раздел: Article
- URL: https://journals.rcsi.science/1068-1620/article/view/229346
- DOI: https://doi.org/10.1134/S1068162019060116
- ID: 229346
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Аннотация
To improve the endothelization of 3D matrices produced by electrospinning we propose adding cyclo(RGDfC) peptide conjugated to human serum albumin (HSA) (HSA-c(RGDfC)) to the electrospinning solution. HSA-c(RGDfC) has been prepared using a bifunctional linker with N-hydroxysuccinimide and maleimide groups, and the product has been confirmed by 1Н NMR spectroscopy. Electrospun matrices have been fabricated from the solutions of 3% polyurethane Tecoflex EG-80A with 10% HSA and 0.01–1.3% HSA–c(RGDfC) (relative to Tec) in 1,1,1,3,3,3-hexafluoro-2-propanol. The presence of HSA and the cyclo(RGDfC) peptide on the surface of electrospun matrices has been confirmed by FTIR spectroscopy. The structure of matrices has been examined by scanning electron microscopy. The ability of the matrices to facilitate the adhesion of primary human umbilical vein endotheliocytes (HUVECs) has been studied. The presence of HSA–c(RGDfC) conjugate in the matrices enhanced cellular adhesion in a dose dependent manner with a maximum effect at 1% HSA-c(RGDfC).
Об авторах
A. Cherepanova
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences; Meshalkin National Medical Research Center, Ministry of Health of the Russian Federation
Автор, ответственный за переписку.
Email: a_cher@niboch.nsc.ru
Россия, Novosibirsk, 630090; Novosibirsk, 630055
D. Akisheva
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences
Email: a_cher@niboch.nsc.ru
Россия, Novosibirsk, 630090
T. Popova
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences; Novosibirsk State University
Email: a_cher@niboch.nsc.ru
Россия, Novosibirsk, 630090; Novosibirsk, 630090
B. Chelobanov
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences; Novosibirsk State University
Email: a_cher@niboch.nsc.ru
Россия, Novosibirsk, 630090; Novosibirsk, 630090
Yu. Chesalov
Boreskov Institute of Catalysis, Federal Research Center, Siberian Branch, Russian Academy of Sciences
Email: a_cher@niboch.nsc.ru
Россия, Novosibirsk, 630090
T. Godovikova
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences; Novosibirsk State University
Email: a_cher@niboch.nsc.ru
Россия, Novosibirsk, 630090; Novosibirsk, 630090
A. Karpenko
Meshalkin National Medical Research Center, Ministry of Health of the Russian Federation
Email: a_cher@niboch.nsc.ru
Россия, Novosibirsk, 630055
P. Laktionov
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences; Meshalkin National Medical Research Center, Ministry of Health of the Russian Federation
Email: a_cher@niboch.nsc.ru
Россия, Novosibirsk, 630090; Novosibirsk, 630055