We present the discovery of innovative low molecular weight inhibitors against human immunodeficiency virus 1 (HIV-1) protease. Structure-based virtual screening focused on potential allosteric surface cavities revealed these compounds [1]. To identify and prioritize such cavities we performed a molecular dynamics simulation were we concentrated on flexible and transient potential binding sites...

The present study characterises an acidic protease purified from the Rhizopus stolonifer strain, RN-11. The acidic protease with a 70 kDa molecular weight, was stable within pH 2-4 at temperatures 40-50°C. The temperature and pH value conducive to optimal catalytic activity were pH 2.5 and 50°C, respectively. Treatment with 5 mmol metal ions showed that the acidic protease was activated by Na, ...

Purified phospholamban isolated from canine cardiac sarcoplasmic reticulum vesicles was subjected to proteolysis and peptide mapping to localize the different sites of phosphorylation on the protein and to gain further information on its subunit structure. Five different proteases (trypsin, papain, chymotrypsin, elastase, and Pronase) degraded the oligomeric 27-kDa phosphoprotein into a major 2...

Photorhabdus luminescens secretes both high molecular weight insecticidal toxin complexes and also a range of extracellular proteases into culture broth. Previous studies by others have suggested that insecticidal activity of the broth is associated with these proteases. However, by gene cloning and targeted knock-out, we have previously shown that oral insecticidal activity is associated with ...

Crystalline hexokinase prepared by the method of Dar-row and Colowick consists largely of enzyme which has been modified in its chromatographic and electrophoretic behavior by yeast protease which is present during the isolation procedure. This proteolytic modification can be prevented by removal of the protease by chromatography on diethylaminoethyl cellulose; it can also be largely inhibited ...

An enzyme from Treponema denticola that hydrolyzes a synthetic trypsin substrate, N-alpha-benzoyl-L-arginine-p-nitroanilide (BAPNA), was purified to near homogeneity, as judged by gel electrophoresis. The molecular weight of the enzyme was estimated to be ca. 69,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and ca. 50,000 by gel filtration on Sephadex G-100. The pH optimum fo...

The interaction between trypsin, a prototype S1 serine protease, with heparin and its low molecular weight derivative dalteparin were investigated. Direct inhibition of the proteolytic activity of trypsin by heparin and dalteparin, used in concentrations typical for their clinical application, was detected. The half-maximum inhibition of the trypsin activity was achieved at 15.25±1.22 μg/mL for...