alpha-chymotrypsin and statine

alpha-chymotrypsin has been researched along with statine* in 2 studies

Other Studies

2 other study(ies) available for alpha-chymotrypsin and statine

Article	Year
A new structural class of selective and non-covalent inhibitors of the chymotrypsin-like activity of the 20S proteasome. Bioorganic & medicinal chemistry letters, 2001, May-21, Volume: 11, Issue:10 We describe the identification and in vitro characterization of a series of 2-aminobenzylstatine derivatives that inhibit non-covalently the chymotrypsin-like activity of the 20S proteasome. Our initial SAR data demonstrate that the 2-aminobenzylstatine core structure can effectively serve as the basis for designing potent, selective and non-covalent inhibitors of the chymotrypsin-like activity of the 20S proteasome. Topics: Amino Acids; Anti-Inflammatory Agents; Antineoplastic Agents; Chymotrypsin; Cysteine Endopeptidases; Enzyme Inhibitors; Humans; Inhibitory Concentration 50; Multienzyme Complexes; Oligopeptides; Peptide Library; Proteasome Endopeptidase Complex; Protein Binding; Structure-Activity Relationship	2001
Novel renin inhibitors containing analogues of statine retro-inverted at the C-termini: specificity at the P2 histidine site. Journal of medicinal chemistry, 1987, Volume: 30, Issue:7 Substituted 1,3- and 1,4-diamines were prepared from epoxides derived from Boc-leucine or Boc-cyclohexylalanine. These diamines were incorporated into renin inhibitors (IC50 = 4-1500 nM) replacing the Leu-Val scissile bond in small peptide analogues of angiotensinogen. Replacement of the P2 histidine imidazole with other heterocycles maintained or enhanced binding while changing the overall basicity of the inhibitor. Finally, substitution of O-methyltyrosine for the P3 phenylalanine suppressed chymotrypsin cleavage of the P3-P2 bond. Topics: Amino Acids; Chymotrypsin; Diamines; Histidine; Humans; Renin; Structure-Activity Relationship	1987

Article

Year

A new structural class of selective and non-covalent inhibitors of the chymotrypsin-like activity of the 20S proteasome.

Bioorganic & medicinal chemistry letters, 2001, May-21, Volume: 11, Issue:10

We describe the identification and in vitro characterization of a series of 2-aminobenzylstatine derivatives that inhibit non-covalently the chymotrypsin-like activity of the 20S proteasome. Our initial SAR data demonstrate that the 2-aminobenzylstatine core structure can effectively serve as the basis for designing potent, selective and non-covalent inhibitors of the chymotrypsin-like activity of the 20S proteasome.

Topics: Amino Acids; Anti-Inflammatory Agents; Antineoplastic Agents; Chymotrypsin; Cysteine Endopeptidases; Enzyme Inhibitors; Humans; Inhibitory Concentration 50; Multienzyme Complexes; Oligopeptides; Peptide Library; Proteasome Endopeptidase Complex; Protein Binding; Structure-Activity Relationship

2001

Novel renin inhibitors containing analogues of statine retro-inverted at the C-termini: specificity at the P2 histidine site.

Journal of medicinal chemistry, 1987, Volume: 30, Issue:7

Substituted 1,3- and 1,4-diamines were prepared from epoxides derived from Boc-leucine or Boc-cyclohexylalanine. These diamines were incorporated into renin inhibitors (IC50 = 4-1500 nM) replacing the Leu-Val scissile bond in small peptide analogues of angiotensinogen. Replacement of the P2 histidine imidazole with other heterocycles maintained or enhanced binding while changing the overall basicity of the inhibitor. Finally, substitution of O-methyltyrosine for the P3 phenylalanine suppressed chymotrypsin cleavage of the P3-P2 bond.

Topics: Amino Acids; Chymotrypsin; Diamines; Histidine; Humans; Renin; Structure-Activity Relationship

1987