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1.
Nat Commun ; 5: 4523, 2014 Jul 25.
Article in English | MEDLINE | ID: mdl-25060339

ABSTRACT

Although electrically stimulated neurite outgrowth on bioelectronic devices is a promising means of nerve regeneration, immunogenic scar formation can insulate electrodes from targeted cells and tissues, thereby reducing the lifetime of the device. Ideally, an electrode material capable of electrically interfacing with neurons selectively and efficiently would be integrated without being recognized by the immune system and minimize its response. Here we develop a cell membrane-mimicking conducting polymer possessing several attractive features. This polymer displays high resistance towards nonspecific enzyme/cell binding and recognizes targeted cells specifically to allow intimate electrical communication over long periods of time. Its low electrical impedance relays electrical signals efficiently. This material is capable to integrate biochemical and electrical stimulation to promote neural cellular behaviour. Neurite outgrowth is enhanced greatly on this new conducting polymer; in addition, electrically stimulated secretion of proteins from primary Schwann cells can also occur on it.


Subject(s)
Biocompatible Materials/chemistry , Biomimetic Materials/chemistry , Neurites/physiology , Animals , Cell Adhesion , Electric Conductivity , Electric Stimulation , Equipment Design , Mice , NIH 3T3 Cells , Nerve Growth Factor/metabolism , Neurons/physiology , PC12 Cells , Peptides/chemistry , Polymers/chemistry , Rats , Schwann Cells
2.
Small ; 10(15): 3012-7, 2014 Aug 13.
Article in English | MEDLINE | ID: mdl-24700425

ABSTRACT

The three-dimensional (3D) poly(3,4-ethylenedioxythiophene) (PEDOT)-based bioelectronic interfaces (BEIs) with diverse dimensional micro/nanorod array structures, varied surface chemical pro-perties, high electrical conductivity, reversible chemical redox switching, and high optical transparency are used for capturing circulating tumor cells (CTCs). Such 3D PEDOT-based BEIs can function as an efficient clinical diagonstic and therapeutic platform.


Subject(s)
Bridged Bicyclo Compounds, Heterocyclic/chemistry , Cell Separation/instrumentation , Conductometry/instrumentation , Nanotubes/chemistry , Neoplastic Cells, Circulating/pathology , Polymers/chemistry , Cell Line, Tumor , Electric Conductivity , Equipment Design , Equipment Failure Analysis , Humans , Miniaturization , Nanotubes/ultrastructure , Surface Properties , Tissue Array Analysis
3.
ACS Nano ; 6(4): 3018-26, 2012 Apr 24.
Article in English | MEDLINE | ID: mdl-22424318

ABSTRACT

Various nanostructures, including nanofibers, nanodots, nanonetwork, and nano- to microsize tubes of functionalized poly(3,4-ethylenedioxythiophene) (EDOT) and poly(3,4-propylenedioxythiophene) (ProDOT) are created by using a template-free electropolymerization method on indium-tin-oxide substrates. By investigating conducting polymer nanostructures containing various functional groups prepared at different polymerization temperature, we conclude a synergistic effect of functional groups and temperature on the formation of polymer nanostructures when a template-free electropolymerization method is applied. For unfunctionalized EDOT and ProDOT, or EDOT containing alkyl functional groups, nanofibers and nanoporous structures are usually found. Interesting, when polar functional groups are attached, conducting polymers tend to form nanodots at room temperature while grow tubular structures at low temperature. The relationship between surface properties and their nanostructures is evaluated by contact angle measurements. The capacity and electrochemical impedance spectroscopy measurements were conducted to understand the electrical properties of using these materials as electrodes. The results provide the relationship between the functional groups, nanostructures, and electrical properties. We also discuss the potential restriction of using this method to create nanostructures. The copolymerization of different functionalized EDOTs may cause irregular and unexpected nanostructures, which indicates the complex interaction between different functionalized monomers during the electropolymerization.

4.
ACS Appl Mater Interfaces ; 4(2): 680-6, 2012 Feb.
Article in English | MEDLINE | ID: mdl-22211371

ABSTRACT

A series of methyl- or benzyl-capped oligoethylene glycol functionalized 2,5-dibromo-3-oxythiophenes are synthesized and successfully polymerized by either Grignard metathesis (GRIM) polymerization or reductive coupling polymerization to yield the corresponding polymers in reasonable yields and molecular weights with narrow molecular weight distribution. These synthesized polyoxythiophenes exhibit high electroactivity and stability in aqueous solution when a potential is applied. Polyoxythiophenes from different polymerization approaches display different colors after purification and spectroelectrochemical studies confirm that the difference of color is from the difference of doping state. Little cytotoxicity is observed for the polymers by in vitro cell compatibility assay. NIH3T3 fibroblast cells are well attached and proliferate on spin-coated films. These results indicate that oligoethylene-glycol-functionalized polyoxythiophenes are promising candidates as conducting biomatierals for biomedical and bioengineering applications.


Subject(s)
Ethylenes/chemistry , Glycols/chemistry , Thiophenes/chemistry , Animals , Catalysis , Cell Engineering , Cell Survival/drug effects , Mice , NIH 3T3 Cells , Polymers/toxicity
6.
ACS Appl Mater Interfaces ; 3(2): 351-9, 2011 Feb.
Article in English | MEDLINE | ID: mdl-21288050

ABSTRACT

Peptides that specifically bind to polyetherimide (PEI) were selected, characterized, and used for the noncovalent modification of the PEI surface. The peptides were successfully identified from a phage-displayed peptide library. A chemically-synthesized peptide composed of the Thr-Gly-Ala-Asp-Leu-Asn-Thr sequence showed an extremely high binding constant for the PEI films (5.6 × 10(8) M(-1)), which was more than three orders of magnitude greater than that for the reference polystyrene films. The peptide was biotinylated and immobilized onto the PEI films to further immobilize streptavidin (SAv). The amount of SAv bound depended on the density of immobilized peptide. It gradually increased with an increasing density of immobilized peptide and achieved a maximum (2.1 pmol cm(-2)) at a peptide density of 19.8 pmol cm(-2). The ratio of peptide used for immobilizing SAv at the maximum value was only 11%, and was partially due to the low accessibility of SAv to the biotin moieties on the PEI films. Moreover, the amount of SAv bound gradually decreased at higher peptide densities, suggesting that the clustering of the peptides also inhibited the binding of SAv. Furthermore, peptides on the PEI films promoted the uniform immobilization of SAv with less structural denaturing. The immobilized SAv was able to further immobilize probe DNA to hybridize with its complementary DNA. These present results suggest that the density of immobilized peptide has a great impact on the surface modifications using polymer-binding peptides.


Subject(s)
Immobilized Proteins/chemistry , Peptides/chemistry , Polymers/chemistry , Amino Acid Sequence , Biotinylation , DNA, Complementary/chemistry , DNA, Complementary/metabolism , Immobilized Proteins/metabolism , Kinetics , Microscopy, Atomic Force , Peptides/metabolism , Polymers/metabolism , Protein Binding , Spectrophotometry, Infrared , Streptavidin/chemistry , Streptavidin/metabolism , Surface Plasmon Resonance , Surface Properties
7.
Langmuir ; 24(13): 6399-403, 2008 Jun 01.
Article in English | MEDLINE | ID: mdl-18500833

ABSTRACT

Short peptides that recognize the alpha form of poly( l-lactide) (PLLA) crystalline films were identified from a phage-displayed peptide library. An enzyme-linked immunosorbent assay (ELISA) revealed that the apparent binding constants of the phage clones for the alpha form of PLLA were greater than those of the unselected phage library. The specificity index for the alpha form of PLLA referred to a structurally similar atactic poly(methyl methacrylate) (at-PMMA), supporting the alpha form of PLLA specific binding of the selected phage. Amino acid residues with proton-donor lateral groups and hydrophobic alkyl groups were relatively enriched in a sequence of heptapeptides on the specific phage clones, thereby suggesting the presence of hydrogen bonding as well as hydrophobic interactions between the alpha form of PLLA and the peptides. Surface plasmon resonance (SPR) analysis revealed that the binding constant of the freed c22 heptapeptide (Gln-Leu-Met-His-Asp-Tyr-Arg) for the alpha form of PLLA was greater than those for reference at-PMMA, amorphous PLLA, and the beta form of PLLA. It was found that c22 peptide can recognize slight differences in PLLA polymorphs such as a crystalline state and an arrangement of PLLA functional groups.


Subject(s)
Peptides/chemistry , Polyesters/chemistry , Amino Acid Sequence , Amino Acids/chemistry , Enzyme-Linked Immunosorbent Assay , Kinetics , Peptide Library , Surface Plasmon Resonance , Surface Properties , Temperature
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