Abstract: Described are compositions and methods for removing one or more host cell proteins from a mixture. The composition comprises one or more peptides wherein each peptide in the composition has a greater binding affinity for the one or more host cell proteins than for one or more target biomolecules.

Abstract: An immunoglobulin binding peptide having the general formula, from amino terminus to carboxy terminus, of Z—R1—R2—R3—R4—R5—R6—X, is described, wherein: R1 is H or Y; R2 is a hydrophobic, preferentially aromatic, amino acid (for example W, F, Y, V); R3 is a positively charged or aromatic amino acid (for example R, H, F, W); R4 is a hydrophobic or positively charged amino acid (for example G, Y, R, K, L); R5 is a positively charged or aromatic amino acid (for example W, F, R, H, Y); R6 a random amino acid but preferably hydrophobic or negatively charged (for example V, W, L, D, H); X is present or absent and when present is a linking group; and Z is present or absent and when present is a capping group bonded to the N terminus of R1; and wherein the amino acids of said peptide are in D form, L form, or a combination thereof.

Abstract: This invention is directed to the discovery of improved methods of preparing cyclic peptides, cyclic peptide esters, cyclic peptide amidines, and libraries of these compounds. The invention also includes uses of these compounds and libraries for screens as drugs and binders of biologics.

Abstract: A biodegradable delivery system for actives such as pharmaceutical drugs. The delivery system includes actives infused into the capsid of a purified plant virus. The loaded capsids are embedding in electrospun biodegradable polymer fibers, forming a nonwoven fabric.

Abstract: A nonwoven fabric has been developed as a delivery system for drugs or other actives which includes biodegradable and biocompatible fibers with plant virus nanoparticles. The plant virus nanoparticles are pre-loaded with one or more actives.

Abstract: An immunoglobulin binding peptide having the general formula, from amino terminus to carboxy terminus, of Z-R1—R2—R3—R4—R5—R6—X, is described, wherein: R1 is H or Y; R2 is a hydrophobic, preferentially aromatic, amino acid (for example W, F, Y, V); R3 is a positively charged or aromatic amino acid (for example R, H, F, W); R4 is a hydrophobic or positively charged amino acid (for example G, Y, R, K, L); R5 is a positively charged or aromatic amino acid (for example W, F, R, H, Y); R6 a random amino acid but preferably hydrophobic or negatively charged (for example V, W, L, D, H); X is present or absent and when present is a linking group; and Z is present or absent and when present is a capping group bonded to the N terminus of R1; and wherein the amino acids of said peptide are in D form, L form, or a combination thereof.

Abstract: An immunoglobulin binding peptide having the general formula, from amino terminus to carboxy terminus, of Z-R1—R2—R3—R4—R5—R6—X, is described, wherein: R1 is H or Y; R2 is a hydrophobic, preferentially aromatic, amino acid (for example W, F, Y, V); R3 is a positively charged or aromatic amino acid (for example R, H, F, W); R4 is a hydrophobic or positively charged amino acid (for example G, Y, R, K, L); R5 is a positively charged or aromatic amino acid (for example W, F, R, H, Y); R6 a random amino acid but preferably hydrophobic or negatively charged (for example V, W, L, D, H); X is present or absent and when present is a linking group; and Z is present or absent and when present is a capping group bonded to the N terminus of R1; and wherein the amino acids of said peptide are in D form, L form, or a combination thereof. Methods of using such peptides for the purification of Immunoglobulins are also described.

Abstract: A method of hydrogenating a polymer comprises: (a) providing a dense phase, the dense phase comprising a polymer in a solvent; (b) providing a catalyst system, the catalyst system comprising as least one metal hydrogenation catalyst (preferably including nickel or ruthenium); and (c) providing a light phase, the light phase comprising, consisting of or consisting essentially of hydrogen and carbon dioxide; and (d) contacting the dense phase, the light phase and the catalyst system under conditions in which the hydrogen reacts with the polymer and hydrogenates the polymer.

Abstract: Environmentally friendly solvents used to dissolve or remove residues and/or substances from substrates wherein the residue and/or substance is contacted with a Generally Recognized As Safe solvent to dissolve the residue and/or substance in the solvent followed by the extraction of the residue and/or substance from the solvent such as by contact with carbon dioxide.

Abstract: The invention provides devices, test kits and methods for removing target agents from a sample. The device contains one or more porous matrices having pore sizes larger than 10 ?m, and a plurality of particles impregnated therein. The target agents attach the device and are removed from the sample.

Abstract: An immunoglobulin binding peptide having the general formula, from amino terminus to carboxy terminus, of Z-R1—R2—R3—R4—R5—R6—X, is described, wherein: R1 is H or Y; R2 is a hydrophobic, preferentially aromatic, amino acid (for example W, F, Y, V); R3 is a positively charged or aromatic amino acid (for example R, H, F, W); R4 is a hydrophobic or positively charged amino acid (for example G, Y, R, K, L); R5 is a positively charged or aromatic amino acid (for example W, F, R, H, Y); R6 a random amino acid but preferably hydrophobic or negatively charged (for example V, W, L, D, H); X is present or absent and when present is a linking group; and Z is present or absent and when present is a capping group bonded to the N terminus of R1; and wherein the amino acids of said peptide are in D form, L form, or a combination thereof.

Abstract: 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.

Abstract: 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.

Abstract: Disclosed are ligands that bind to regions of the prion peptide and methods of using same.

Abstract: A method of reducing undesired topographic features, increasing film density, and/or increasing adhesion to an underlying substrate in a polymer film formed on a microelectronic substrate, comprises: (a) providing a microelectronic substrate, the substrate having a polymer film deposited thereon; (b) contacting the substrate to carbon dioxide (optionally containing additional ingredients such as cosolvents or chemical intermediates); and (c) elevating the pressure of the carbon dioxide to plasticize the polymer film and reduce undesired topographic features, increase film density, and/or increase adhesion of the film to the underlying substrate.