RGD Peptide–Albumin Conjugate for Endothelization of Electrospun Materials
- Authors: Cherepanova A.V.1,2, Akisheva D.1, Popova T.V.1,3, Chelobanov B.P.1,3, Chesalov Y.A.4, Godovikova T.S.1,3, Karpenko A.A.2, Laktionov P.P.1,2
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Affiliations:
- 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
- Issue: Vol 45, No 6 (2019)
- Pages: 793-802
- Section: Article
- URL: https://journals.rcsi.science/1068-1620/article/view/229346
- DOI: https://doi.org/10.1134/S1068162019060116
- ID: 229346
Cite item
Abstract
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).
About the authors
A. V. 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
Author for correspondence.
Email: a_cher@niboch.nsc.ru
Russian Federation, 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
Russian Federation, Novosibirsk, 630090
T. V. Popova
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences; Novosibirsk State University
Email: a_cher@niboch.nsc.ru
Russian Federation, Novosibirsk, 630090; Novosibirsk, 630090
B. P. Chelobanov
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences; Novosibirsk State University
Email: a_cher@niboch.nsc.ru
Russian Federation, Novosibirsk, 630090; Novosibirsk, 630090
Yu. A. Chesalov
Boreskov Institute of Catalysis, Federal Research Center, Siberian Branch, Russian Academy of Sciences
Email: a_cher@niboch.nsc.ru
Russian Federation, Novosibirsk, 630090
T. S. Godovikova
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences; Novosibirsk State University
Email: a_cher@niboch.nsc.ru
Russian Federation, Novosibirsk, 630090; Novosibirsk, 630090
A. A. Karpenko
Meshalkin National Medical Research Center, Ministry of Health of the Russian Federation
Email: a_cher@niboch.nsc.ru
Russian Federation, Novosibirsk, 630055
P. 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
Russian Federation, Novosibirsk, 630090; Novosibirsk, 630055