Abstract: Novel inhibitors of metalloproteases are disclosed. Such compounds are useful in pharmaceutical compositions and methods for treating or controlling disease states or conditions which involve tissue breakdown, such as rheumatoid arthritis.

Abstract: Peptides of 10 to 40 or more amino acid residues in length and having the sequence X3X4X5GPX6TWX7X8 (SEQ ID NO:252) where each amino acid is indicated by standard one letter abbreviation; X3 is C; X4 is R, H, L, or W; X.sub.5 is M, F, or I; X6 is independently selected from any one of the 20 genetically coded L-amino acids; X7 is D, E, I, L, or V; and X8 is C, which bind and activate the erythropoietin receptor (EPO-R) or otherwise act as an EPO agonist, and methods for their use.

Abstract: Biotinylation peptides can be fused to other peptides or proteins of interest using recombinant DNA techniques to provide efficient methods for biotinylating the resulting fusion proteins in vivo or in vitro.

Abstract: Novel inhibitors of metalloproteases, in particular collagenase-1 and stromelysin-1, are disclosed. Such compounds are useful in pharmaceutical compositions and methods for treating or controlling disease states or conditions which involve tissue breakdown, such as rheumatoid arthritis.

Abstract: Disclosed are novel inhibitors of metalloproteases, in particular matrix metalloproteases. The disclosed inhibitors are mercaptoketone and mercaptoalcohol compounds which are useful in pharmaceutical compositions and methods for treating or controlling disease states or conditions which involve tissue breakdown, for example, arthropathy, dermatological conditions, bone resorption, inflammatory diseases, and tumor invasion and in the promotion of wound healing.

Abstract: Improved methods and novel compositions for identifying peptides and single-chain antibodies that bind to predetermined receptors or epitopes. Such peptides and antibodies are identified by improved and novel methods for affinity screening of polysomes displaying nascent peptides.

Abstract: Novel compounds are provided which are useful as photocleavable linking groups in solid phase synthesis. Compositions incorporating these linking groups and methods for their use are also described.

Abstract: Peptides that bind to the interleukin-1 type I receptor (IL-1RtI) can be used to assay the amount of IL-1R, or an IL-1R agonist or antagonist, in a sample and comprise a sequence of amino acids selected from the group consisting of (1) WXXXGZ.sub.1 W where Z.sub.1 is L, I, A, or Q (SEQ ID NO:2); (2) XXQZ.sub.5 YZ.sub.6 XX where Z.sub.5 is P or Aze where Aze is azetidine; and Z.sub.6 is S, A, V, or L (SEQ ID NO:1); and (3) Z.sub.23 NZ.sub.24 SZ.sub.25 Z.sub.26 Z.sub.27 Z.sub.28 Z.sub.29 Z.sub.30 L where Z.sub.23 is D or Y; Z.sub.24 is D or S; Z.sub.25 is S or W; Z.sub.26 is S or Y; Z.sub.27 is D or V; Z.sub.28 is S or W; Z.sub.29 is F or L; and Z.sub.30 is D or L (SEQ ID NO:27); and where each amino acid is indicated by standard one letter abbreviation; and each X can be selected from any one of the 20 genetically coded L-amino acids or the stereoisomeric D-amino acids.

Abstract: Biotinylation peptides can be fused to other peptides or proteins of interest using recombinant DNA techniques to provide efficient methods for biotinylating the resulting fusion proteins in vivo or in vitro.

Abstract: Peptides that bind to the interleukin-1 type I receptor (IL-1RtI) can be used to assay the amount of IL-1R, or an IL-1R agonist or antagonist, in a sample and comprise a sequence of amino acids selected from the group consisting of (1) WXXXGZ.sub.1 W where Z.sub.1 is L, I, A, or Q; (2) XXQZ.sub.5 YZ.sub.6 XX where Z.sub.5 is P or Aze where Aze is azetidine; and Z.sub.6 is S, A, V, or L; and (3) Z.sub.23 NZ.sub.24 SZ.sub.25 Z.sub.26 Z.sub.27 Z.sub.28 Z.sub.29 Z.sub.30 L where Z.sub.23 is D or Y; Z.sub.24 is D or S; Z.sub.25 is S or W; Z.sub.26 is S or Y; Z.sub.27 is D or V; Z.sub.28 is S or W; Z.sub.29 is F or L; and Z.sub.30 is D or L; and where each amino acid is indicated by standard one letter abbreviation; and each X can be selected from any one of the 20 genetically coded L-amino acids or the stereoisomeric D-amino acids. Also provided are peptides which bind to the IL-1RtI, which are 11 to 40 amino acids in length, which comprise the core sequence of amino acids:Z.sub.31 XWZ.sub.32 Z.sub.33 Z.sub.34 Z.

Abstract: Disclosed are novel inhibitors of collagenase-1 and stromelysin-I metalloproteases. The disclosed inhibitors are mercaptoketone and mercaptoalcohol compounds which are useful in pharmaceutical compositions and methods for treating or controlling disease states or conditions which involve tissue breakdown, for example, arthropathy, dermatological conditions, bone resorption, inflammatory diseases, and tumor invasion and in the promotion of wound healing.

Abstract: Peptides of 10 to 40 or more amino acid residues in length and having the sequence X.sub.3 X.sub.4 X.sub.5 GPX.sub.6 TWX.sub.7 X.sub.8 (SEQ ID NO:252) where each amino acid is indicated by standard one letter abbreviation; X.sub.3 is C; X.sub.4 is R, H, L, or W; X.sub.5 is M, F, or I; X.sub.6 is independently selected from any one of the 20 genetically coded L-amino acids; X.sub.7 is D, E, I, L, or V; and X.sub.8 is C, which bind and activate the erythropoietin receptor (EPO-R) or otherwise act as an EPO agonist, and methods for their use.

Abstract: A method for generating libraries of displayed peptides and/or antibodies (Abs) suitable for affinity interaction screening or phenotypic screening comprising: (i) obtaining selected library members comprising a displayed peptide and/or Ab and the corressponding polynucleotide (PN), or copies of it, (ii) pooling and fragmenting the PN, or copies of it, to form fragments, (iii) performing PCR amplification and thereby homologously recombining the fragments to form a shuffled pool of recombined PNs, which are not present in the selected library of (i).

Abstract: Disclosed are novel inhibitors of metalloproteases, in particular matrix metalloproteases. The disclosed inhibitors are mercaptoketone and mercaptoalcohol compounds which are useful in pharmaceutical compositions and methods for treating or controlling disease states or conditions which involve tissue breakdown, for example, arthropathy, dermatological conditions, bone resorption, inflammatory diseases, and tumor invasion and in the promotion of wound healing.

Abstract: The present invention relates to the areas of organic and medicinal chemistry. More specifically, the present invention is concerned with combinatorial and solid phase methods for the synthesis of diverse diketopiperazine derivatives, and the use of such methods to create libraries of diverse diketopiperazine derivatives. The present invention has application in the areas of chemical synthesis, the screening for new diketopiperazine derivatives having beneficial medical properties and the use of such screening to provide compositions and methods including diketopiperazine derivatives for treating disease.

Abstract: PTH analogs comprising an amino acid sequence that is: SVSEIQLLHNX.sub.1 X.sub.2 X.sub.3 HX.sub.4 X.sub.3 X.sub.3 X.sub.3 X.sub.5 RVX.sub.5 WLR X.sub.4 X.sub.4 LX.sub.3 X.sub.3 VX.sub.1 X.sub.3 X.sub.3 X (SEQ ID NO:10) wherein X.sub.1 is a neutral or positively charged amino acid, X.sub.2 is a neutral amino acid, X.sub.3 is a neutral, positively charged, or negatively charged amino acid, X.sub.4 is a positively charged amino acid, X.sub.5 is a positively charged or negatively charged amino acid, and X is selected from the group consisting of Hol, Ho, a homoserine amide, or the sequence of amino acids comprising residues 35-84 of PTH, have enhanced activity and increased serum half-life as compared with human PTH. The PTH analogs can be produced as fusion proteins in high yields in E. coli host cells; the fusion proteins can be subsequently cleaved to produce the PTH analog.

Abstract: A method for DNA reassembly after random fragmentation, and its application to mutagenesis of nucleic acid sequences by in vitro or in vivo recombination is described. In particular, a method for the production of nucleic acid fragments or polynucleotides encoding mutant proteins is described. The present invention also relates to a method of repeated cycles of mutagenesis, shuffling and selection which allow for the directed molecular evolution in vitro or in vivo of proteins.

Abstract: A general stochastic method for synthesizing random oligomers on particles is disclosed. A further aspect of the invention relates to the use of identification tags on the particles to facilitate identification of the sequence of the monomers in the oligomer.

Abstract: Disclosed are peptides and peptide mimetics that bind selectins, including endothelial leukocyte adhesion molecule 1 (ELAM-1). Such peptides and peptide mimetics are useful in methods for blocking adhesion of leukocytes to the selectins for the purpose of inhibiting inflammation as well as in diagnostic methods employing labeled peptides and peptide mimetics that bind selectins for the purpose of determining the site of inflammation in mammals which inflammation is mediated by the presence of one or more selectins.

Abstract: Peptides that bind to the interleukin-1 type I receptor (IL-1RtI) can be used to assay the amount of IL-1R, or an IL-1R agonist or antagonist, in a sample and comprise a sequence of amino acids selected from the group consisting of (1) WXXXGZ.sub.1 W where Z.sub.1 is L, I, A, or Q; (2) XXQZ.sub.5 YZ.sub.6 XX where Z.sub.5 is P or Aze where Aze is azetidine; and Z.sub.6 is S, A, V, or L; and (3) Z.sub.23 NZ.sub.24 SZ.sub.25 Z.sub.26 Z.sub.27 Z.sub.28 Z.sub.29 Z.sub.30 L where Z.sub.23 is D or Y; Z.sub.24 is D or S; Z.sub.25 is S or W; Z.sub.26 is S or Y; Z.sub.27 is D or V; Z.sub.28 is S or W; Z.sub.29 is F or L; and Z.sub.30 is D or L; and where each amino acid is indicated by standard one letter abbreviation; and each X can be selected from any one of the 20 genetically coded L-amino acids or the stereoisomeric D-amino acids. Also provided are peptides which bind to the IL-1RtI, which are 11 to 40 amino acids in length, which comprise the core sequence of amino acids:Z.sub.31 XWZ.sub.32 Z.sub.33 Z.sub.34 Z.