Abstract: Provided herein are methods of detecting and diagnosing types of amyloid-related diseases. Also provided herein are methods of treatment comprising selecting a treatment based upon a particular type of amyloid disease.

Abstract: Provided herein are antibody-peptide fusion proteins comprising an amyloid-reactive peptide linked to an antibody. Also provided herein are methods of treating amyloid-based diseases by administering an antibody-peptide fusion protein.

Abstract: Provided herein are modified immunoglobulins comprising an amyloid reactive peptide joined to an antibody, as well as humanized antibodies that bind to human amyloid fibrils and antibody-peptide fusion proteins. Also provided herein are methods of treating amyloid-based diseases by administering a modified immunoglobulin, humanized antibody, or antibody-peptide fusion protein.

Abstract: Provided herein are chimeric receptors comprising amyloid binding regions, as well as cells comprising the chimeric receptors. Also provided herein are methods of treating amyloid-based diseases by administering a cell comprising a chimeric receptor.

Abstract: Provided herein are modified immunoglobulins comprising an amyloid reactive peptide joined to an antibody, as well as humanized antibodies that bind to human amyloid fibrils and antibody-peptide fusion proteins. Also provided herein are methods of treating amyloid-based diseases by administering a modified immunoglobulin, humanized antibody, or antibody-peptide fusion protein.

Abstract: Immunoglobulin light chain proteins are used to generate synthetic fibrils in vitro. The fibrils are mixed with immunoglobulin light chain proteins from a biological sample. In either a direct binding assay, competition assay, or dilution-based competition assay, a signal is detected from the mixture. The intensity of the detectable signal relates to the level of binding between the immunoglobulin light chain proteins to the fibrils and can thus be used to identify amyloidogenic immunoglobulin light chain proteins in a biological sample of the subject and to assess amyloidogenic risk to a subject. For example, the signal intensities from the assays can be used in a comparison to one or more threshold (control) values derived from samples of known light chain types or in the absence of light chains. The comparisons permit identification of amyloidogenic proteins, assessment of amyloidogenic risk, and categorization of the subject into an appropriate “at risk” group.

Abstract: Disclosed are methods and compositions for targeting antibodies to amyloid deposits. For example, amyloid-reactive peptides that bind amyloid deposits are administered to a subject. Antibodies to the amyloid-reactive peptides are then administered to the subject. Upon administration of the antibodies, the amyloid-reactive peptides bind the antibodies and thus pre-target the antibodies to the amyloid deposits. In other examples, an amyloid-reactive fusion peptide contains an epitope of a known antibody. When the fusion peptide is administered to a subject, the fusion peptide binds amyloids in the subject. Administration to the subject of the known antibody that binds the epitope of the fusion peptide then targets the antibody to the amyloid deposit to which the fusion peptide is bound.

Abstract: Disclosed are methods of treating and/or inhibiting a viral infection in a subject. The methods include administering a therapeutically effective amount of heparin-binding peptide. Also disclosed herein are methods for blocking viral binding to a cell. Further disclosed are anti-viral compositions for administration to a subject infected with a virus. Administration of the anti-viral composition inhibits viral infection of the subject.

Abstract: Disclosed are methods and compositions for targeting antibodies to amyloid deposits. For example, amyloid-reactive peptides that bind amyloid deposits are administered to a subject. Antibodies to the amyloid-reactive peptides are then administered to the subject. Upon administration of the antibodies, the amyloid-reactive peptides bind the antibodies and thus pre-target the antibodies to the amyloid deposits. In other examples, an amyloid-reactive fusion peptide contains an epitope of a known antibody. When the fusion peptide is administered to a subject, the fusion peptide binds amyloids in the subject. Administration to the subject of the known antibody that binds the epitope of the fusion peptide then targets the antibody to the amyloid deposit to which the fusion peptide is bound.

Abstract: Disclosed are methods and compositions for targeting antibodies to amyloid deposits. For example, amyloid-reactive peptides that bind amyloid deposits are administered to a subject. Antibodies to the amyloid-reactive peptides are then administered to the subject. Upon administration of the antibodies, the amyloid-reactive peptides bind the antibodies and thus pre-target the antibodies to the amyloid deposits. In other examples, an amyloid-reactive fusion peptide contains an epitope of a known antibody. When the fusion peptide is administered to a subject, the fusion peptide binds amyloids in the subject. Administration to the subject of the known antibody that binds the epitope of the fusion peptide then targets the antibody to the amyloid deposit to which the fusion peptide is bound.

Abstract: Immunoglobulin light chain proteins are used to generate synthetic fibrils in vitro. The fibrils are mixed with immunoglobulin light chain proteins from a biological sample. In either a direct binding assay, competition assay, or dilution-based competition assay, a signal is detected from the mixture. The intensity of the detectable signal relates to the level of binding between the immunoglobulin light chain proteins to the fibrils and can thus be used to identify amyloidogenic immunoglobulin light chain proteins in a biological sample of the subject and to assess amyloidogenic risk to a subject. For example, the signal intensities from the assays can be used in a comparison to one or more threshold (control) values derived from samples of known light chain types or in the absence of light chains. The comparisons permit identification of amyloidogenic proteins, assessment of amyloidogenic risk, and categorization of the subject into an appropriate “at risk” group.

Abstract: Disclosed are methods and compositions for targeting antibodies to amyloid deposits. For example, amyloid-reactive peptides that bind amyloid deposits are administered to a subject. Antibodies to the amyloid-reactive peptides are then administered to the subject. Upon administration of the antibodies, the amyloid-reactive peptides bind the antibodies and thus pre-target the antibodies to the amyloid deposits. In other examples, an amyloid-reactive fusion peptide contains an epitope of a known antibody. When the fusion peptide is administered to a subject, the fusion peptide binds amyloids in the subject. Administration to the subject of the known antibody that binds the epitope of the fusion peptide then targets the antibody to the amyloid deposit to which the fusion peptide is bound.

Abstract: Disclosed are methods and compositions for targeting antibodies to amyloid deposits. For example, amyloid-reactive peptides that bind amyloid deposits are administered to a subject. Antibodies to the amyloid-reactive peptides are then administered to the subject. Upon administration of the antibodies, the amyloid-reactive peptides bind the antibodies and thus pre-target the antibodies to the amyloid deposits. In other examples, an amyloid-reactive fusion peptide contains an epitope of a known antibody. When the fusion peptide is administered to a subject, the fusion peptide binds amyloids in the subject. Administration to the subject of the known antibody that binds the epitope of the fusion peptide then targets the antibody to the amyloid deposit to which the fusion peptide is bound.

Abstract: Disclosed are methods of treating and/or inhibiting a viral infection in a subject. The methods include administering a therapeutically effective amount of heparin-binding peptide. Also disclosed herein are methods for blocking viral binding to a cell. Further disclosed are anti-viral compositions for administration to a subject infected with a virus. Administration of the anti-viral composition inhibits viral infection of the subject.

Abstract: Disclosed are methods of treating and/or inhibiting a viral infection in a subject. The methods include administering a therapeutically effective amount of heparin-binding peptide. Also disclosed herein are methods for blocking viral binding to a cell. Further disclosed are anti-viral compositions for administration to a subject infected with a virus. Administration of the anti-viral composition inhibits viral infection of the subject.

Abstract: Disclosed are methods and compositions for targeting antibodies to amyloid deposits. For example, amyloid-reactive peptides that bind amyloid deposits are administered to a subject. Antibodies to the amyloid-reactive peptides are then administered to the subject. Upon administration of the antibodies, the amyloid-reactive peptides bind the antibodies and thus pre-target the antibodies to the amyloid deposits. In other examples, an amyloid-reactive fusion peptide contains an epitope of a known antibody. When the fusion peptide is administered to a subject, the fusion peptide binds amyloids in the subject. Administration to the subject of the known antibody that binds the epitope of the fusion peptide then targets the antibody to the amyloid deposit to which the fusion peptide is bound.

Abstract: Disclosed are methods of treating and/or inhibiting a viral infection in a subject. The methods include administering a therapeutically effective amount of heparin-binding peptide. Also disclosed herein are methods for blocking viral binding to a cell. Further disclosed are anti-viral compositions for administration to a subject infected with a virus. Administration of the anti-viral composition inhibits viral infection of the subject.

Abstract: The present invention provides a method of purifying cross-linked oligomers. The purified cross-linked oligomers are useful as immunogen for generating and isolating cross-linked oligomer reactive antibodies. The cross-linked oligomer reactive antibodies are useful for detecting amyloid deposition and for diagnosing and treating diseases and conditions associated with amyloid deposition.

Abstract: The present invention provides IGIV and IGIV enriched for binding to amyloid fibrils and to partially denatured amyloidogenic precursor polypeptides. The present invention also provides methods for obtaining IGIV enriched for binding to amyloid fibrils and to partially denatured amyloidogenic precursor polypeptides. The IGIV recognizes amyloid fibrils and partially denatured amyloidogenic precursor polypeptides. They are useful for treating diseases and conditions associated with amyloid deposition. The IGIV of the present invention also are useful for diagnosing and detecting amyloid deposition.

Abstract: Disclosed are methods of treating and/or inhibiting a viral infection in a subject. The methods include administering a therapeutically effective amount of heparin-binding peptide. Also disclosed herein are methods for blocking viral binding to a cell. Further disclosed are anti-viral compositions for administration to a subject infected with a virus. Administration of the anti-viral composition inhibits viral infection of the subject.