PMID- 18237156
OWN - NLM
STAT- MEDLINE
DCOM- 20080609
LR  - 20171116
IS  - 0003-2700 (Print)
IS  - 0003-2700 (Linking)
VI  - 80
IP  - 5
DP  - 2008 Mar 1
TI  - Long-term affinity modification on poly(dimethylsiloxane) substrate and its 
      application for ELISA analysis.
PG  - 1529-35
LID - 10.1021/ac7020618 [doi]
AB  - Poly(dimethylsiloxane) (PDMS) possesses many advantages, such as biocompatibility 
      and high oxygen permeability, which makes it an attractive material for 
      fabricating biodevices. Creating an affinity surface with long-term stability and 
      reactivity for biomolecular interactions on a PDMS substrate, however, is 
      difficult due to its inherent hydrophobicity. In this study, an affinity surface 
      on a PDMS substrate with long-term hydrophilicity and affinity reactivity is 
      reported. This modification is composed of two parts. The bottom part is made of 
      polyelectrolyte multilayers and is capable of providing long-term hydrophilic 
      stability. The top part consists of three protein layers, bovine serum albumin 
      (BSA), anti-BSA, and protein G, and offers an affinity surface for antibody 
      binding and, more importantly, provides favorable orientation and minimum 
      nonspecific binding. The chemical modification for the different stages was 
      monitored by atomic force microscopy (AFM), attenuated total reflection Fourier 
      transform infrared spectroscopy (ATR-FT-IR), and contact angle and fluorescence 
      measurements. A long-term PDMS immunodevice (LPID) based on polyelectrolyte 
      multilayers and protein layers was fabricated and applied to the detection of 
      transforming growth factor beta (TGF-beta) protein in mouse serum by the 
      enzyme-linked immunosorbent assay (ELISA) method. Results show that a linear 
      calibration curve was obtained in the concentration range from 500 to 15.125 
      pg/mL, and the relative standard deviation was less than 3%. Also, the amount of 
      TGF-beta spiked in mouse serum was precisely determined. Results indicate that 
      the modified surface was hydrophilic and reactive to biospecies up to more than 7 
      days in its dry form. Moreover, the blocking reagent used to reduce nonspecific 
      binding was found to be not necessary for the LPID. Thus, the reported method is 
      expected to hold a great potential for fabricating PDMS-based affinity devices 
      such as protein chips.
FAU - Sung, Wang-Chou
AU  - Sung WC
AD  - Department of Chemistry, and Department of Environmental and Occupational Health, 
      National Cheng Kung University, Tainan, 701, Taiwan.
FAU - Chang, Chih-Ching
AU  - Chang CC
FAU - Makamba, Honest
AU  - Makamba H
FAU - Chen, Shu-Hui
AU  - Chen SH
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20080201
PL  - United States
TA  - Anal Chem
JT  - Analytical chemistry
JID - 0370536
RN  - 0 (Dimethylpolysiloxanes)
RN  - 0 (Silicones)
RN  - 27432CM55Q (Serum Albumin, Bovine)
RN  - 63148-62-9 (baysilon)
SB  - IM
MH  - Dimethylpolysiloxanes/*chemistry
MH  - Enzyme-Linked Immunosorbent Assay/*instrumentation
MH  - Microscopy, Atomic Force
MH  - Protein Binding
MH  - Serum Albumin, Bovine/chemistry
MH  - Silicones/*chemistry
MH  - Surface Properties
EDAT- 2008/02/02 09:00
MHDA- 2008/06/10 09:00
CRDT- 2008/02/02 09:00
PHST- 2008/02/02 09:00 [pubmed]
PHST- 2008/06/10 09:00 [medline]
PHST- 2008/02/02 09:00 [entrez]
AID - 10.1021/ac7020618 [doi]
PST - ppublish
SO  - Anal Chem. 2008 Mar 1;80(5):1529-35. doi: 10.1021/ac7020618. Epub 2008 Feb 1.