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Cell adhesion, spreading, and proliferation on surface functionalized with RGD nanopillar arrays

Authors
Kafi, Md. AbdulEl-Said, Waleed AhmedKim, Tae-HyungChoi, Jeong-Woo
Issue Date
Jan-2012
Publisher
ELSEVIER SCI LTD
Keywords
Three-dimensional peptide nanostructures; Cell-substrate interaction; RGD peptide; Cell functions; Cofilin phosphorylation
Citation
BIOMATERIALS, v.33, no.3, pp 731 - 739
Pages
9
Journal Title
BIOMATERIALS
Volume
33
Number
3
Start Page
731
End Page
739
URI
https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/43493
DOI
10.1016/j.biomaterials.2011.10.003
ISSN
0142-9612
1878-5905
Abstract
In this paper, a method was introduced for the fabrication of vertically and spatially-controlled peptide nanostructures that enhance cell adhesion, proliferation, spreading on artificial surfaces. The RGD nanostructures with different heights were fabricated on gold surfaces by self-assembly technique through a nanoporous alumina mask composed of nanoscale-controlled pores. Pore diameter and spatial distribution were controlled by manipulating the pore widening time at a constant voltage during the mask fabrication process. Two-dimensional RGD nanodot, three-dimensional RGD nanorod, and RGD nanopillar arrays were carried out using various concentrations of RGD peptide solution, self-assembly times, and pore sizes, which were 74 nm, 63 nm, and 43 nm in diameter, respectively. The fabricated RGD nanodot, nanorod, and nanopillar arrays were utilized as a cell adhesion layer to evaluate the cell adhesion force, adhesion speed, spreading assay, and phosphorylation of cofilin protein in PC12, HeLa, and HEK293T normal cells. Among the three different nanostructures, RGD nanopillar arrays were found to be suitable for cellular attachment, spreading, and proliferation due to the proper arrangement of the RGD motif, which mimics in vivo conditions. Hence, our newly fabricated RGD nanostructured array can be successfully applied as a bio-platform for improving cellular functions and in in vitro tissue engineering. (C) 2011 Elsevier Ltd. All rights reserved.
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