Standard

In vitro modeling of cell-scaffold interaction. / Korzhikov, V. A.; Vlakh, E. G.; Kasper, C.; Tennikova, T. B.

In: Russian Journal of Bioorganic Chemistry, Vol. 37, No. 3, 01.05.2011, p. 270-276.

Research output: Contribution to journal › Article › peer-review

Harvard

Korzhikov, VA, Vlakh, EG, Kasper, C & Tennikova, TB 2011, 'In vitro modeling of cell-scaffold interaction', Russian Journal of Bioorganic Chemistry, vol. 37, no. 3, pp. 270-276. https://doi.org/10.1134/S1068162011020087

APA

Korzhikov, V. A., Vlakh, E. G., Kasper, C., & Tennikova, T. B. (2011). In vitro modeling of cell-scaffold interaction. Russian Journal of Bioorganic Chemistry, 37(3), 270-276. https://doi.org/10.1134/S1068162011020087

Vancouver

Korzhikov VA, Vlakh EG, Kasper C, Tennikova TB. In vitro modeling of cell-scaffold interaction. Russian Journal of Bioorganic Chemistry. 2011 May 1;37(3):270-276. https://doi.org/10.1134/S1068162011020087

Author

Korzhikov, V. A. ; Vlakh, E. G. ; Kasper, C. ; Tennikova, T. B. / In vitro modeling of cell-scaffold interaction. In: Russian Journal of Bioorganic Chemistry. 2011 ; Vol. 37, No. 3. pp. 270-276.

BibTeX

@article{c264c946273b471b9979073165c33d2d,
title = "In vitro modeling of cell-scaffold interaction",
abstract = "A simple method of controlling the efficiency of surface ligand-cell receptor interaction has been developed in the course of modeling the specific adhesion of cells on a support with their subsequent proliferation and bone tissue formation, using affinity chromatography on macroporous monolithic sorbents. The biospecific peptide GRGDSP played the role of an active ligand on the support, whereas cells were simulated by polymeric (polystyrene) microparticles with the peptide EDYPVDIYYLMDLSYSMKDD immobilized on their surface. The latter peptide is part of the active site of the integrin molecule responsible for binding the RGD sequence. Thus, the monolithic ultrashort column (CIM{\textregistered} disk) represented a simplified model of the support (structural scaffold) possessing biospecific properties. The parameters of the interaction of affinity partners were quantitatively estimated by frontal analysis involving the construction of adsorption isotherms, followed by their linearization and mathematical processing. The data obtained indicate a high specificity of biological pairing, which is supported by the results of cell culture experiments.",
keywords = "affinity chromatography, modeling of cellular interactions, tissue engineering",
author = "Korzhikov, {V. A.} and Vlakh, {E. G.} and C. Kasper and Tennikova, {T. B.}",
year = "2011",
month = may,
day = "1",
doi = "10.1134/S1068162011020087",
language = "English",
volume = "37",
pages = "270--276",
journal = "Russian Journal of Bioorganic Chemistry",
issn = "1068-1620",
publisher = "МАИК {"}Наука/Интерпериодика{"}",
number = "3",

}

RIS

TY - JOUR

T1 - In vitro modeling of cell-scaffold interaction

AU - Korzhikov, V. A.

AU - Vlakh, E. G.

AU - Kasper, C.

AU - Tennikova, T. B.

PY - 2011/5/1

Y1 - 2011/5/1

N2 - A simple method of controlling the efficiency of surface ligand-cell receptor interaction has been developed in the course of modeling the specific adhesion of cells on a support with their subsequent proliferation and bone tissue formation, using affinity chromatography on macroporous monolithic sorbents. The biospecific peptide GRGDSP played the role of an active ligand on the support, whereas cells were simulated by polymeric (polystyrene) microparticles with the peptide EDYPVDIYYLMDLSYSMKDD immobilized on their surface. The latter peptide is part of the active site of the integrin molecule responsible for binding the RGD sequence. Thus, the monolithic ultrashort column (CIM® disk) represented a simplified model of the support (structural scaffold) possessing biospecific properties. The parameters of the interaction of affinity partners were quantitatively estimated by frontal analysis involving the construction of adsorption isotherms, followed by their linearization and mathematical processing. The data obtained indicate a high specificity of biological pairing, which is supported by the results of cell culture experiments.

AB - A simple method of controlling the efficiency of surface ligand-cell receptor interaction has been developed in the course of modeling the specific adhesion of cells on a support with their subsequent proliferation and bone tissue formation, using affinity chromatography on macroporous monolithic sorbents. The biospecific peptide GRGDSP played the role of an active ligand on the support, whereas cells were simulated by polymeric (polystyrene) microparticles with the peptide EDYPVDIYYLMDLSYSMKDD immobilized on their surface. The latter peptide is part of the active site of the integrin molecule responsible for binding the RGD sequence. Thus, the monolithic ultrashort column (CIM® disk) represented a simplified model of the support (structural scaffold) possessing biospecific properties. The parameters of the interaction of affinity partners were quantitatively estimated by frontal analysis involving the construction of adsorption isotherms, followed by their linearization and mathematical processing. The data obtained indicate a high specificity of biological pairing, which is supported by the results of cell culture experiments.

KW - affinity chromatography

KW - modeling of cellular interactions

KW - tissue engineering

UR - http://www.scopus.com/inward/record.url?scp=79960148043&partnerID=8YFLogxK

U2 - 10.1134/S1068162011020087

DO - 10.1134/S1068162011020087

M3 - Article

AN - SCOPUS:79960148043

VL - 37

SP - 270

EP - 276

JO - Russian Journal of Bioorganic Chemistry

JF - Russian Journal of Bioorganic Chemistry

SN - 1068-1620

IS - 3

ER -

ID: 35888765