Abstract: The present invention relates to a novel class of &agr;-aminoboronic acids of Formula (V), which are useful as intermediates in synthetic processes for inhibitors of the serine proteases, leukocyte elastase, pancreatic elastase, cathepsin G, and chymotrypsin. More specifically, the &agr;-aminoboronic acids are useful as intermediates for the synthesis of Hepatitis C Virus (HCV) protease inhibitors. This invention also generally relates to novel methods for the preparation of &agr;-aminoboronic acids.

Abstract: This invention relates to a novel method of hepatitis C protease inhibition through interaction with a novel exosite remote from the active site but overlapping with P4′-P6′ region of the extended substrate binding site. In particular, the present invention provides a description of a region of the enzyme and structure activity relationships of peptides with affinity for this exosite. Ligands binding in the exosite are competitive with larger substrates such as the physiological substrate. As such, exploitation of the exosite represents a therapeutic for the hepatitis C disease.

Abstract: The present invention relates to the discovery of new C-terminal boronic acid dipeptide inhibitors of trypsin-like enzymes such as thrombin and pharmaceutical compositions thereof.

Abstract: A method for the removal of ester protecting groups from .alpha.-amino boronic acid is disclosed for the preparation of compounds of formula (II) belowR.sup.1 -X.sub.n -NHCH (R.sup.2)-B(OH).sub.

Abstract: Intermediates for the preparation of Peptides comprising C-terminal boronic acid derivatives of lysine, ornithine, and arginine, homoarginine and corresponding isothiouronium analogs thereof, are reversible inhibitors of trypsin-like serine proteases such as thrombin, plasma kallikrein and plasmin.

Abstract: Peptides comprising C-terminal boronic acid derivatives of lysine, ornithine, and arginine, homoarginine and corresponding isothiouronium analogs thereof, are reversible inhibitors of trypsin-like serine proteases such as thrombin, plasma kallikrein and plasmin.

Abstract: Peptides comprising C-terminal boronic acid derivatives of lysine, ornithine, and arginine, homoarginine and corresponding isothiouronium analogs thereof, are reversible inhibitors of trypsin-like serine proteases such as thrombin, plasma kallikrein and plasmin.

Abstract: A method for preparing selected peptide substrates for detecting the activity of virus-specified proteases is provided. Specific tetrapeptide substrates are disclosed which are conjugates of protease-cleavable indicator groups and peptide sequences resembling picornavirus protease cleavage recognition sites.

Abstract: A compound having the structure ##STR1## where T is of the fomrula ##STR2## where each D.sup.1 and D.sup.2, independently, is a hydroxyl group of a group which is capable of being hydrolysed to a hydroxyl group in aqueous solution at physiological pH; a group of the formula ##STR3## where G is either H,F or an alkyl group containing 1 to about 20 carbon atoms and optional heteroatoms which can be N, S, or O; or a phosphonate group of the formula ##STR4## where J is O-alkyl, N-alkyl, or alkyl, each comprising about 1-20 carbon atoms and, optionally, heteroatoms which can be N, S, or O; T being able to form a complex with the catalytic site of an enzyme, X is a group having at least one amino acid, ##STR5## and each R.sup.1, R.sup.2, R.sup.3, R.sup.4, R.sup.5, R.sup.6, R.sup.7, and R.sup.8 is separately a group which does not interfere significantly (i.e., does not lower than Ki of the compound to less than 10.sup.

Abstract: Certain peptide methyl ketone derivatives inhibit picornavirus replication by inhibition of virus-specified protease activity.

Abstract: A general method for preparing specific inhibitors of virus-specified proteases is disclosed. The inhibitors comprise a halomethyl ketone or methyl ketone moiety covalently linked to a peptide sequence of three, four or five amino acids or amino acid residues, which peptide sequence corresponds to an amino acid sequence found adjacent to and upstream of a cleavage site recognized by a virus-specified protease.

Abstract: Selected tripeptide and tetrapeptide halomethyl ketones are employed in processes for treating viral infection in mammals. These compounds inhibit picornavirus protease activity.

Abstract: Peptide and amino acid halomethyl ketones are employed in processes for inhibiting cyclic nucleotide independent protein kinase activity and tumor cell growth.

Abstract: Peptides comprising C-terminal .alpha.-aminoboronic acid residues are potent, reversible inhibitors of proteolytic enzymes.

Abstract: A peptide affinity label of the formula (I): ##STR1## wherein X is a radical capable of acting as a leaving group in a nucleophilic substitution reaction;A is an aromatic amino acid residue;B is H, or a C.sub.1 -C.sub.4 alkyl group, or aryl;Y is selected from the group consisting of hydrogen, aroyl, C.sub.1 -C.sub.6 acyl, and Q--(A)--.sub.n, whereinQ=hydrogen, aroyl, or C.sub.1 -C.sub.6 acyl,n=1-10,A is an amino acid residue selected from the aliphatic, hydroxy-containing, carboxylic acid group, and amide-thereof-containing, aromatic, sulfur-containing and imino-containing amino acids; and wherein J is selected from the group consisting of --CH.sub.2 --, --CH.sub.2 --CH.sub.2 --,--CH.sub.2 --CH.sub.2 --CH.sub.2 --, --CH.dbd.CH-- and --CH(OH)--CH.sub.2. The affinity label is useful for irreversibly inactivating thrombin and trypsin-like enzymes and may be used as a potential anticlotting agent.