			Home About us Contact

Specific Capture (specific + capture)

Distribution by Scientific Domains

Chemistry	60%

Selected Abstracts

Ring-Opening Polymerization with Synergistic Co-monomers: Access to a Boronate-Functionalized Polymeric Monolith for the Specific Capture of cis -Diol-Containing Biomolecules under Neutral Conditions,

ANGEWANDTE CHEMIE, Issue 36 2009
Lianbing Ren
Molekulare Teamarbeit: Synergistische Comonomere in einem Boronat-funktionalisierten Polymermonolithen wirken wie ein einzelner Boronsäureligand vom Wulff-Typ und ermöglichen die spezifische Bindung von cis -Diol-Biomolekülen unter neutralen Bedingungen (siehe Schema). Beim Ansäuern des Mediums wird die Aminogruppe protoniert und die B-N-Koordination aufgehoben, was zur Freisetzung des cis -Diols vom Monolithen führt. [source]

A micropillar-integrated smart microfluidic device for specific capture and sorting of cells

ELECTROPHORESIS, Issue 24 2007
Yan-Jun Liu
Abstract An integrated smart microfluidic device consisting of nickel micropillars, microvalves, and microchannels was developed for specific capture and sorting of cells. A regular hexagonal array of nickel micropillars was integrated on the bottom of a microchannel by standard photolithography, which can generate strong induced magnetic field gradients under an external magnetic field to efficiently trap superparamagnetic beads (SPMBs) in a flowing stream, forming a bed with sufficient magnetic beads as a capture zone. Fluids could be manipulated by programmed controlling the integrated air-pressure-actuated microvalves, based on which in situ bio-functionalization of SPMBs trapped in the capture zone was realized by covalent attachment of specific proteins directly to their surface on the integrated microfluidic device. In this case, only small volumes of protein solutions (62.5,nL in the capture zone; 375,nL in total volume needed to fill the device from inlet A to the intersection of outlet channels F and G) can meet the need for protein! The newly designed microfluidic device reduced greatly chemical and biological reagent consumption and simplified drastically tedious manual handling. Based on the specific interaction between wheat germ agglutinin (WGA) and N -acetylglucosamine on the cell membrane, A549 cancer cells were effectively captured and sorted on the microfluidic device. Capture efficiency ranged from 62 to 74%. The integrated microfluidic device provides a reliable technique for cell sorting. [source]

Chemical Micropatterning of Polycarbonate for Site-Specific Peptide Immobilization and Biomolecular Interactions

CHEMBIOCHEM, Issue 3 2007
Olivier Carion Dr.
Abstract Polycarbonate (PC) is a useful substrate for the preparation of microfluidic devices. Recently, its utility in bioanalysis has attracted much attention owing to the possibility of using compact discs as platforms for the high-throughput analysis of biomolecular interactions. In this article we report a novel method for the chemical micropatterning of polycarbonate based on the printing of functionalized silica nanoparticles. The semicarbazide groups present on the surface of the nanoparticles were used for the site-specific semicarbazone ligation of unprotected peptides derivatized by an ,-oxoaldehyde group. The peptide micropatterns permitted the specific capture of antibodies. We report also the characterization of micropatterns on PC by using a wide-field optical imaging technique called Sarfus; this allows the detection of nm-thick films by using nonreflecting PC substrates and an optical microscope working with reflected differential interference contrast. The method described here is an easy way to modify polycarbonate surfaces for biomolecular interaction studies and should stimulate the use of PC for developing plastic biosensors. [source]

Protein Engineering Strategies for Selective Protein Purification

CHEMICAL ENGINEERING & TECHNOLOGY (CET), Issue 11 2005
M. Hedhammar
Abstract When producing and purifying recombinant proteins it is of importance to minimize the number of unit operations during the purification procedure. This is accomplished by increasing the selectivity in each step. Due to the high selectivity of affinity chromatography it has a widespread use in protein purification. However, most target proteins lack a suitable affinity ligand usable for capture on a solid matrix. A way to circumvent this obstacle is to genetically fuse the gene encoding the target protein with a gene encoding a purification tag. When the chimeric protein is expressed, the tag allows for specific capture of the fusion protein. In industrial-scale production, extension of the target protein often is unwanted since it might interfere with the function of the target protein. Hence, a purification scheme developed for the native protein is desired. In this review, different fusion strategies used for protein purification are discussed. Also, the development of ligands for selective affinity purification of native target proteins is surveyed. [source]