Perseptive Biosystems Inc.

Purdue Research Foundation

Fred B Regnier

Noubar Boghos Afeyan

Laszlo Varady

Satish Jindal

Bing He

Sandeep K Paliwal

David Evans

Kevin Williams

Aruna Pingali

A method for protein identification in complex mixtures that utilizes affinity selection of constituent proteolytic peptide fragments unique to a protein analyte. These 'signature peptides' function as analytical surrogates. Mass spectrometric analysis of the proteolyzed mixture permits identification of a protein in a complex sample without purifying the protein or obtaining its composite peptide signature.

Affinity selected signature peptides for protein identification and quantification

The invention provides novel methods for screening a sample to select a ligand to a target of interest and for obtaining information about the ligand and its binding characteristics. Specifically, the claimed multi-dimensional methods involve combining a solution of heterogeneous ligands with the target of interest to screen the ligands on the basis of one or more binding characteristics. Ligands having the first binding characteristic bind to the target of interest thereby to form a target/ligand complex. The complex then optionally is separated from the unbound components using any of a variety of separation techniques, e.g., size exclusion. At least one of the complex or unbound components then is introduced to a second &ldquo;dimension&rdquo;. The second dimension is capable of separating components based upon a second binding characteristic. One then elutes the ligand having the desired binding characteristics.

High speed, automated, continuous flow, multi-dimensional molecular selection and analysis

The present invention relates to an in situ micromachined mixer for microfluidic analytical systems. In a preferred embodiment, a 100 pL mixer for liquids transported by electroosmotic flow (EOF) is described. Mixing was achieved in multiple intersecting channels with a bimodal width distribution and varying lengths. Five &mgr;m width channels ran parallel to the direction of flow whereas larger 27 &mgr;m width channels ran back and forth through the network at a 45&deg; angle. All channels were approximately 10 &mgr;m deep. It was observed that little mixing of confluent streams occurred in the 100 &mgr;m wide mixer inlet channel where mixing would be achieved almost exclusively by diffusion. In contrast, mixing was complete after passage through the channel network in the &ap;200 &mgr;m length mixer. Solvent composition was altered by varying the voltage on solvent reservoirs. The high efficiency attained in this mixer was attributed to the presence of a 2 pL vortex in the center of the mixer. Video tracking of fluorescent particles with a fluorescence microscope allowed the position and volume of this vortex to be determined.

In situ micromachined mixer for microfluidic analytical systems

Disclosed are chemically-produced specific binding, 'molecular imaged' sorbents which reversibly bind a preselected macromolecule by spatially matched multipoint interactions between functional groups synthesized on the surface of the sorbent and functional groups on the surface of the macromolecule. Also disclosed are methods of producing such sorbents. The sorbents typically are high surface area solids comprising surface binding regions which have charged groups, metal coordinating groups, hydrophobic moieties, or various combination thereof anchored thereto and spaced in the mirror image of complementary interactive groups on a surface of the macromolecule.

Molecular imaging

Disclosed are chemically-produced specific binding, 'molecular imaged' sorbents which reversibly bind a preselected macromolecule by spacially matched multipoint interactions between functional groups synthesized on the surface of the sorbent and functional groups on the surface of the macromolecule. Also disclosed are methods of producing such sorbents. The sorbents typically are high surface area solids comprising surface binding regions which have charged groups, metal coordinating groups, hydrophobic moities, or various combination thereof anchored thereto and spaced in the mirror image of complementary interactive groups on a surface of the macromolecule.

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West Lafayette, IN, United States of America

Fred B Regnier