Abstract: The invention provides AFTI polypeptides and nucleic acid molecules encoding the same. The invention also provides vectors, host cells, selective binding agents, and methods for producing AFTI polypeptides. Also provided are methods for the treatment, diagnosis, amelioration, or prevention of diseases with AFTI polypeptides, particularly IL-1 mediated diseases, TNF-? mediated diseases, and diseases involving monocyte activation.

Abstract: The present invention concerns therapeutic agents that mimic the activity of Apo-AI amphipathic helix peptide. In accordance with the present invention, the compounds of the invention comprise: a. a Apo-AI amphipathic helix peptide or Apo-AI amphipathic helix peptide-mimetic domain, preferably the amino acid sequence of SEQ ID NO: 7, or sequences derived therefrom by phage display, RNA-peptide screening, or the other techniques mentioned above; and b. a vehicle, such as a polymer (e.g., PEG or dextran) or an Fc domain, which is preferred; wherein the vehicle, preferably an Fc domain, is covalently attached to the Apo-AI amphipathic helix peptide or Apo-AL amphipathic helix peptide-mimetic domain. The vehicle and the Apo-AI amphipathic helix peptide or Apo-AI amphipathic helix peptide-mimetic domain may be linked through the N- or C-terminus of the Apo-AI amphipathic helix peptide or Apo-AI amphipathic helix peptide-mimetic domain, as described further below.

Abstract: Biologically active conjugates are disclosed which are formed by reaction of a thiol moiety of a biologically active molecule with a non-peptidic polymer having an active sulfone moiety. Also disclosed are compounds having the formula R1—X—R2 wherein at least one of R1 and R2 is a biologically active molecule having a reactive thiol moiety which forms a covalent bond with X, a Michael acceptor-activated non-peptidic polymer. Further disclosed are methods of making the conjugates and compounds of the present invention as well as pharmaceutical compositions containing them. In addition, activated polymers suitable for attachment to a variety of molecules and surfaces are disclosed.

Abstract: Compounds are disclosed having the general formula R1-X-R2, wherein R1 and R2 are biologically active groups, at least one of which is polypeptidic. X is a non-peptidic polymeric group. R1 and R2 may be the same or different. Preferred R1 and R2 groups are TNF inhibitors.

Abstract: The present invention provides nucleic acid molecules encoding a 30kDa TNF inhibitor or a fragment thereof having at least one non-native cysteine residue at the N-terminus, C-terminus, residue 14, or residue 15.

Abstract: The present invention concerns therapeutic agents that mimic the activity of Apo-AI amphipathic helix peptide.

Abstract: The present invention concerns fusion of half-life extending vehicles, preferably Fc domains, with peptide sequences that act as antagonists of integrins, selectins, cell adhesion molecules, or their respective receptors. Linkage to the vehicle increases the half-life of the peptide, which otherwise would be quickly degraded in vivo. The peptide may be an existing peptide or a peptide selected by phage display, E. coli display, ribosome display, RNA-peptide screening, chemical-peptide screening, or other methods.

Abstract: The invention provides AFTI polypeptides and nucleic acid molecules encoding the same. The invention also provides vectors, host cells, selective binding agents, and methods for producing AFTI polypeptides. Also provided are methods for the treatment, diagnosis, amelioration, or prevention of diseases with AFTI polypeptides, particularly IL-1 mediated diseases, TNF-&agr; mediated diseases, and diseases involving monocyte activation.

Abstract: At least two substantially purified tumor necrosis factor (TNF) inhibitors are disclosed which are glycoproteins that are active against TNF. The isolation of 3O kDa and 40 KDa TNF inhibitor from urine is disclosed. The deglycosylated form of the 3O kDa TNF inhibitor and 40 kDa TNF inhibitor are described as being active against TNF. The 40 kDa TNF inhibitor is active against both TNF alpha a TNF beta. The amino acid sequence of the 30 kDa TNF inhibitor and the 40 kDa TNF inhibitor are disclosed. Methods for isolating the TNF inhibitors from human U937 cell medium and producing the proteins by recombinant-DNA methods are also described.

Abstract: This invention describes processes for producing mature human members of the NGF/BDNF family of neurotrophic proteins that are fully biologically active. In addition, the gene encoding human BDNF and human BDNF are disclosed. A previously-unreported member of the NGF/BDNF family of neurotrophic proteins, NGF-3, has been identified and a portion of the gene encoding for the NGF-3 has been described.

Abstract: A process for the production of biologically active recombinant neurotrophic factor from the NGF/BDNF family is described. The process is comprised of a) constructing a synthetic neurotrophic factor gene suitable for expression in a bacterial expression system; b) the synthetic neurotrophic factor gene is expressed in a bacterial expression system; c) the neurotrophic factor is solubilized and sulfonylated; d) sulfonylated neurotrophic factor is allowed to refold in the presence of polyethylene glycol and urea; and e) biologically active neurotrophic factor is isolated and purified.

Abstract: This invention describes processes for producing mature human members of the NGF/BDNF family of neurotrophic proteins that are fully biologically active. In addition, the gene encoding human BDNF and processes for obtaining the same are disclosed.A previously-unreported member of the NGF/BDNF family of neurotrophic proteins, NGF-3, has been identified and a portion of the gene encoding for the NGF-3 has been described. Processes for identifying additional previously unreported members of the NGF/BDNF family are also described.