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.
| Original language | English |
|---|---|
| Pages (from-to) | 3808-3817 |
| Number of pages | 10 |
| Journal | Soft Matter |
| Volume | 7 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - 2011 Apr 21 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Chemistry(all)
- Condensed Matter Physics
Cite this
}
Attachment and morphology of adipose-derived stromal cells and exposure of cell-binding domains of adsorbed proteins on various self-assembled monolayers. / Chieh, Hsiao Feng; Su, Fong-chin; Liao, Jiunn-Der; Lin, Sheng Che; Chang, Chia Wei; Shen, Meng-Ru.
In: Soft Matter, Vol. 7, No. 8, 21.04.2011, p. 3808-3817.Research output: Contribution to journal › Article
TY - JOUR
T1 - Attachment and morphology of adipose-derived stromal cells and exposure of cell-binding domains of adsorbed proteins on various self-assembled monolayers
AU - Chieh, Hsiao Feng
AU - Su, Fong-chin
AU - Liao, Jiunn-Der
AU - Lin, Sheng Che
AU - Chang, Chia Wei
AU - Shen, Meng-Ru
PY - 2011/4/21
Y1 - 2011/4/21
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=79953734696&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=79953734696&partnerID=8YFLogxK
U2 - 10.1039/c1sm05172e
DO - 10.1039/c1sm05172e
M3 - Article
VL - 7
SP - 3808
EP - 3817
JO - Soft Matter
JF - Soft Matter
SN - 1744-683X
IS - 8
ER -