NDLI: Attachment and morphology of adipose-derived stromal cells and exposure of cell-binding domains of adsorbed proteins on various self-assembled monolayers

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Soft Matter Vol - 7 Issue - 7

Soft Matter Vol - 7 Issue - 6

Soft Matter Vol - 7 Issue - 5

Soft Matter Vol - 7 Issue - 4

Soft Matter Vol - 7 Issue - 3

Attachment and morphology of adipose-derived stromal cells and exposure of cell-binding domains of adsorbed proteins on various self-assembled monolayers

Content Provider	Royal Society of Chemistry (RSC)
Author	Liao, Jiunn-Der Shen, Meng-Ru Su, Fong-Chin Chieh, Hsiao-Feng Chang, Chia-Wei Lin, Sheng-Che
Copyright Year	2011
Abstract	Self-assembled monolayers (SAMs) of alkanethiols, 1-decanethiol (DT10), 11-mercapto-1-undecanol (MUOH), 11-mercapto-undecanoic acid (MUA), and 11-amino-1-undecanethiol (AUT), terminated with methyl (–CH3), hydroxyl (–OH), carboxyl (–COOH), and amino (–NH2) groups, were chemically adsorbed on Au and used as substrate surfaces. The features of the SAMs adsorbed on Au were characterized using physicochemical and depth-sensing nano-indentation methods. The ordering of various tail-group terminated SAMs on Au was associated with the rate of harmonic contact stiffness of the SAM molecules along with the measured displacement (MUA/Au < AUT/Au ≈ MUOH/Au < DT10/Au). However, the slight difference in nano-mechanical properties among SAMs/Au does not reach the variation required to induce cellular mechano-sensitive responses. Immunostaining analyses of cytoskeleton indicate that initial adipose-derived stromal cell (ADSCs) attachment and cell morphology on SAMs/Au was regulated by the surface chemistry. The effects of surface chemistry on the exposed cell-binding domains of adsorbed bovine fibronectin (bFN) and bovine vitronectin (bVN) under single-protein or multi-protein conditions were also examined to determine the most potent protein for ADSC attachement. The results reveal that under the single-protein condition, the exposed cell-binding domains of both bFN and bVN on SAMs/Au follow the sequence of tail-groups, –NH2, –COOH, –OH, and –CH3. However, SAMs with the tail-group –CH3 behaved significantly differently. Under the multi-protein condition, bFN domains showed a different sequence of tail-groups, –OH, –NH2 ≈ –COOH, and –CH3, whereas bVN domains showed the same sequence as that for the single-protein condition. Results of cell behavior and the exposed cell-binding domains of adhesive proteins suggest that vitronectin might be the fundamental adhesive protein for mediating ADSC attachment and spreading.
Starting Page	3808
Ending Page	3817
Page Count	10
File Format	HTM / HTML PDF
ISSN	1744683X
Volume Number	7
Issue Number	8
Journal	Soft Matter
DOI	10.1039/c1sm05172e
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Harmonic Immunohistochemistry Auckland University of Technology Contact mechanics Vitronectin ADSC The Features Fibronectin Protein Hydroxy group Carboxylic acid MUA Self-assembled monolayer Cytoskeleton Surface science Stromal cell
Content Type	Text
Resource Type	Article
Subject	Chemistry Condensed Matter Physics

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