American National Red Cross

North Carolina State University

Pathogen Removal and Diagnostic Technologies Inc.

Bio-rad Laboratories, Inc.

Prometic Biosciences Inc.

Pathogen Removal and Diagnostics Technologies Inc.

David John Hammond

Ruben Guillermo Carbonell

Julia Tait Lathrop

Steven James Burton

Larisa Cervenakova

Patrick Vasconcelos Gurgel

Honglue Shen

Egisto Boschetti

Annemarie H Ralston

Baldev Singh Baines

Viterose Wiltshire-Lyerly

Iwona Fijalkowska

Billy L Kolen

Serguei Soukharev

Viteros Wiltshire-Lyerly

Timothy Keith Hayes

Dwun-Hou Chen

Christopher Bryant

John Curling

Baldev Baines

Ligands that bind to prion proteins and methods for using the ligands for detecting or removing a prion protein from a sample, such as a biological fluid or an environmental sample. The ligands are capable of binding to one or more forms of prion protein including cellular prion protein (PrPc), infectious prion protein (PrPsc), and recombinant prion protein (PrPr). Prions from various species, including humans and hamsters, are bound by the ligands. Also provided is a method of treating or retarding the development of a prion-associated pathology in a subject.

Prion protein ligands and methods of use

The present invention relates to the fields of molecular biology, combinatorial chemistry and biochemistry. Particularly, the present invention describes methods and kits for dynamically reducing the variance between analyte taken from complex mixtures.

Methods for reducing the range in concentrations of analyte species in a sample

The invention discloses methods for sequential protein isolation and purification from a biological sample by affinity chromatography. Affinity chromatography is conducted using ligands or ligand support complexes that selectively and specifically bind to proteins in the biological sample. The ligands or ligand support complexes were contacted sequentially in a predetermined order with the biological sample to allow each ligand or ligand-support complex to sequentially bind a protein from the biological sample.

Sequential protein isolation and purification schemes by affinity chromatography

Prion protein binding materials and methods for using the binding materials to detect or remove a prion protein from a sample, such as a biological fluid or an environmental sample. The binding materials are capable of binding to one or more forms of prion protein including cellular prion protein (PrPc), infectious prion protein (PrPsc), recombinant prion protein (PrPr), and proteinase resistant prion protein (PrPres). Prions from various species, including humans and hamsters, are bound by the binding materials.

Prion protein binding materials and methods of use

Disclosed are compounds of the formula (I): wherein R, R, R, R, and Rare selected from the group consisting of H and groups or atoms other than H, and Rand Rare halo or hydrogen; X, X, and Xare independently O or S; provided that Rand Rare not simultaneously H, when all of X, X, and Xare O; and of the formula (II) wherein R-Rare selected from the group consisting of H and groups or atoms other than H; X-Xare independently O or S; n and m are 0 or 1 but m and n cannot be 0 simultaneously; R-Rcan be H or any substituent so long as the compound of formula II upon hydrolysis provides a fluorescent compound. These compounds are useful as substrates with high specificity for organophosphatase particularly human paraoxonase and bacterial organophosphorus hydrolase. Also disclosed is a method for detecting and/or measuring the paraoxonase activity in a fluid comprising contacting the fluid with a fluorescent substrate and measuring the fluorescence of the fluorescent product formed. 

Fluorescent substrates for detecting organophosphatase enzyme activity

The present invention provides a method for purifying butyrylcholinesterase from various biological fluids. Biological fluids include, e.g., blood, blood fractions, plasma, and bioreactor broths, and other such mixtures containing butyrylcholinesterase. In one embodiment, the invention provides a method for the production of purified, virally inactivated butyrylcholinesterase by contacting a biological fluid containing butyrylcholinesterase with a cationic exchange chromatography material, with an affinity chromatography material, and treating the fluid with solvent detergent. The resulting purified butyrylcholinesterase can also be subjected to a pasteurization step, and formulated in a sodium chloride/sodium phosphate solution for storage or lyophilization.

Method for the production of pure virally inactivated butyrylcholinesterase

The invention provides an isolated or purified peptide that binds at least one plasma protein. In one embodiment, the isolated or purified peptide binds to fibrinogen, comprises no more than 10 amino acids, and comprises an amino acid sequence Xaa-Xaa-Xaa-Xaa-Xaa, an amino acid sequence Gly-Xaa-Arg-Xaa, or an amino acid sequence selected from specific amino acid sequences provided herein. Alternatively, the isolated or purified protein binds to &#x3b1;l proteinase inhibitor and/or a protein complex comprising Apo-A1 lipoprotein and paraoxonase. The peptide comprises no more than 10 amino acids and comprises an amino acid sequence Xaa-Xaa-Xaa-His-Xaa-Xaa, and amino acid sequence His-Xaa-Xaa-Xaa-Xaa-Xaa, or an amino acid sequence selected from specific amino acid sequences provided herein. In addition, the invention provides isolated or purified peptide that binds to von Willebrand Factor. The peptide comprises an amino acid sequence Xaa-Xaa-Xaa, an amino acid sequence Tyr-Leu-Xaa-Xaa-Xaa-Thr, or an amino acid sequence selected from specific amino acid sequences provided herein.

Plasma protein-binding ligands

The invention provides a method of characterizing a target that binds to a ligand. The method comprises providing ligands, optionally attached to a support, and contacting the ligands with targets to allow at least one target to bind to at least one ligand. The method further comprises immobilizing the resulting complexes in a first matrix, such that each complex has a different position within the first matrix, and transferring the target of the complex to a second matrix. The position of the target within the second matrix corresponds to the position of the ligand-support complex within the first matrix. The target on the second matrix is then detected.

Method for detecting ligands and targets in a mixture

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Laytonsville, MD, United States of America

David John Hammond