PMID- 25966872
OWN - NLM
STAT- MEDLINE
DCOM- 20160303
LR  - 20150602
IS  - 1520-5827 (Electronic)
IS  - 0743-7463 (Linking)
VI  - 31
IP  - 21
DP  - 2015 Jun 2
TI  - Surface Modification of Poly(dimethylsiloxane) Using Ionic Complementary Peptides 
      to Minimize Nonspecific Protein Adsorption.
PG  - 5891-8
LID - 10.1021/acs.langmuir.5b01085 [doi]
AB  - Poly(dimethylsiloxane) (PDMS) has become a widely used material for microfluidic 
      and biological applications. However, PDMS has unacceptably high levels of 
      nonspecific protein adsorption, which significantly lowers the performance of 
      PDMS-based microfluidic chips. Most existing methods to reduce protein fouling of 
      PDMS are to make the surface more hydrophilic by surface oxidization, polymer 
      grafting, and physisorbed coatings. These methods suffer from the relatively 
      short-term stability, the multistep complex treatment procedure, or the 
      insufficient adsorption reduction. Herein, we developed a novel and facile 
      modification method based on self-assembled peptides with well-tailored amino 
      acid composition and sequence, which can also interact strongly with the PDMS 
      surface in the same way as proteins, for suppressing the nonspecific protein 
      fouling and improving the biocompatibility of PDMS-based microfluidic chips. We 
      first demonstrated that an ionic complementary peptide, EAR16-II with a sequence 
      of [(Ala-Glu-Ala-Glu-Ala-Arg-Ala-Arg)2], can readily self-assemble into an 
      amphipathic film predominantly composed of tightly packed beta-sheets on the native 
      hydrophobic and plasma-oxidized hydrophilic PDMS surfaces upon low concentrations 
      of carbohydrates. The self-assembled EAR16-II amphipathic film exposed its 
      hydrophobic side to the solution and thus rendered the PDMS surface hydrophobic 
      with water contact angles (WCAs) of around 110.0 degrees . However, the self-assembled 
      EAR16-II amphipathic film exhibited excellent protein-repelling and blood 
      compatibility properties comparable to or better than those obtained with 
      previously reported methods. A schematic model has been proposed to explain the 
      interactions of EAR16-II with the PDMS surface and the antifouling capability of 
      EAR16-II coatings at a molecular level. The current work will pave the way to the 
      development of novel coating materials to address the nonspecific protein 
      adsorption on PDMS, thereby broadening the potential uses of PDMS-based 
      microfluidic chips in complex biological analysis.
FAU - Yu, Xiaoling
AU  - Yu X
AD  - Key Laboratory of Analytical Chemistry for Life Science of Shaanxi Province, 
      School of Chemistry and Chemical Engineering, Shaanxi Normal University, 620 West 
      Chang'an Street, Xi'an 710119, China.
FAU - Xiao, Junzhu
AU  - Xiao J
AD  - Key Laboratory of Analytical Chemistry for Life Science of Shaanxi Province, 
      School of Chemistry and Chemical Engineering, Shaanxi Normal University, 620 West 
      Chang'an Street, Xi'an 710119, China.
FAU - Dang, Fuquan
AU  - Dang F
AD  - Key Laboratory of Analytical Chemistry for Life Science of Shaanxi Province, 
      School of Chemistry and Chemical Engineering, Shaanxi Normal University, 620 West 
      Chang'an Street, Xi'an 710119, China.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20150520
PL  - United States
TA  - Langmuir
JT  - Langmuir : the ACS journal of surfaces and colloids
JID - 9882736
RN  - 0 (Dimethylpolysiloxanes)
RN  - 0 (Peptides)
RN  - 0 (Proteins)
RN  - 63148-62-9 (baysilon)
SB  - IM
MH  - Adsorption
MH  - Dimethylpolysiloxanes/*chemistry
MH  - Hydrophobic and Hydrophilic Interactions
MH  - Microfluidics
MH  - Peptides/chemistry
MH  - Proteins/*chemistry
EDAT- 2015/05/15 06:00
MHDA- 2016/03/05 06:00
CRDT- 2015/05/14 06:00
PHST- 2015/05/14 06:00 [entrez]
PHST- 2015/05/15 06:00 [pubmed]
PHST- 2016/03/05 06:00 [medline]
AID - 10.1021/acs.langmuir.5b01085 [doi]
PST - ppublish
SO  - Langmuir. 2015 Jun 2;31(21):5891-8. doi: 10.1021/acs.langmuir.5b01085. Epub 2015 
      May 20.