North Carolina State University

Pathogen Removal and Diagnostic Technologies Inc.

Prometic Biosciences Inc.

Patrick Vasconcelos Gurgel

Ruben Guillermo Carbonell

Steven James Burton

David John Hammond

Honglue Shen

James Christopher Pearson

Yong Zheng

Helen Rosemary Tatton

Haiou Yang

Viteros Wiltshire-Lyerly

Viterose Wiltshire-Lyerly

Haiyan Liu

Samana Roy Chowdhury

David J Hammond

Sumana Roy Chowdhury

The present invention describes a novel process for the conformal coating of polymer fibers of nonwoven substrates. This process is based on modification of polymer fiber surfaces by controlling the degree of etching and oxidation to improve adhesion of initiators to the surface and to facilitate subsequent conformal polymer grafting. The modified fiber surfaces render new functionalities to the surface, such as increased hydrophilicity, attached ligands or changed surface energy. The invention includes the modified polymer fibers produced by the process described herein.

Conformal coating of polymer fibers on nonwoven substrates

Compounds of formula (I) wherein Rand Rare the same or different and are each optionally substituted alkyl, optionally substituted cycloalkyl, optionally substituted aryl or optionally substituted heteroaryl groups; Ris hydrogen or an aryl group substituent or Ris a solid support optionally attached via a spacer; Z represents an oxygen atom, a sulphur atom or NR; Y represents an oxygen atom, a sulphur atom or NR; in which Rand R, which may be the same or different, represent hydrogen, optionally substituted alkyl containing 1 to 6 carbon atoms, optionally substituted phenyl, optionally substituted benzyl or optionally substituted &#x3b2;-phenylethyl; and one of Xand Xrepresents a nitrogen atom and the other of Xand Xrepresents a nitrogen atom or CR, in which Rrepresents hydrogen or an aryl group substituent; are useful for the affinity binding of a prion protein. 

Substituted triazines as prion protein ligands and their use to detect or remove prions

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

An immunoglobulin binding peptide having the general formula, from amino terminus to carboxy terminus, of Z-R&#x2014;R&#x2014;R&#x2014;R&#x2014;R&#x2014;R&#x2014;X, is described, wherein: Ris H or Y; Ris a hydrophobic, preferentially aromatic, amino acid (for example W, F, Y, V); Ris a positively charged or aromatic amino acid (for example R, H, F, W); Ris a hydrophobic or positively charged amino acid (for example G, Y, R, K, L); Ris a positively charged or aromatic amino acid (for example W, F, R, H, Y); Ra 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 R; 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.

Purification of immunoglobulins using affinity chromatography and peptide ligands

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Cary, NC, United States of America

Patrick Vasconcelos Gurgel