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.

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: 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.