HomeClass Notes1,200,000CA670,000

PCL102H1 Lecture 6: Structure-based Drug Development

60 views2 pages

lemonhamster432

31 Jan 2019

School

Department

Pharmacology and Toxicology

Course

Professor

For unlimited access to Class Notes, a Class+ subscription is required.

Document Summary

Lecture 6: structure-based drug development and improving your chemical compounds. X-ray crystallography: technique used for determining the atomic and molecular structure of a crystal. Xrc can be used to identify structure of protein: start with small amount of very conc. Some proteins of interest for drug discovery are the 15 proteins of the hiv virus - many of the proteins are vital to the hiv life cycle (e. g. enzymes, structural proteins, accessory proteins, etc. ) Hiv protease is an important protein, two molecules are required to form the active enzyme. Tipranavir & saquinavir is an example of an hiv protease inhibitor drug. One normal version of hiv protease, but thousands of mutants, drug-resistant version of hiv protease = due to muations in hiv genome. So how do we develop drugs for the mutant forms: answer: one possibility might be screen drugs virtually, against all mutant forms of the enzyme.

Related Documents

PCL102H1 Lecture Notes - Lecture 16: Drug Design, Hiv-1 Protease, X-Ray Crystallography

ceruleanwater-buffalo592

PCL102H1 Lecture Notes - Lecture 19: Hiv-1 Protease, X-Ray Crystallography, Drug Design

PCL102H1 Lecture 6: Structure-Based Drug Development & Improving Your Chemical Compound

Related Questions

Can you please answer my questions fast I appreciate it no explanation is needed

B. C. Mixed tive 8. The panereas is protected from digestion by trypsin (a proteolytic enzyme that it produces) because: A. B. C. D. Trypsin works only on denatured proteins Trypsin is specific for plant proteins Trypsin works only at the surface of membranes Trypsin is not activated until it is proteolytically modified 9. The active site of an enzyme is the region that A. binds allosteric regulators of the enzyme. B. is involved in the catalytic reaction of the enzyme C. binds noncompetitive inhibitors of the enzyme D. is inhibited by the presence of a coenzyme or a cofactor 10. According to the induced fit hypochesis of enzyme catalysis,which of the following is corect? A. The binding of the substrate depends on the shape of the active site B. Some enzymes change their structure when activators bind to the enzyme C. A competitive inhibitor can outcompete the substrate for the active site D. The binding of the substrate changes the shape of the enzyme's active site 11. Increasing the substrate concentration in an enzymatic reaction could overcome which of the following? A. denaturization of the enzyme B. allosteric inhibition C competitive inhibition D. saturation of the enzyme activity 12. Zinc, an essential trace element for most organisms, is present in the active site of the enzyme carboxypeptidase. The zinc most likely functions as a(n) A. competitive inhibitor of the enzyme B. noncompetitive inhibitor of the enzyme C. allosteric activator of the enzyme. D cofactor necessary for enzyme activity 13. Some of the drugs used to treat HIV patients are competitive inhibitors of the HIV reverse transcriptase enzyme. Unfortunately, the high mutation rate of HIV means that the virus rapidly acquires mutations with amino acid changes that make them resistant to these competitive inhibitors. Where in the reverse transcriptase enzyme would such amino acid changes most likely occur in drug-resistant viruses? A. in or near the active site B. at an allosteric site Cat a cofactor binding site D. in regions of the protein that determine packaging into the virus capsid the fever is not controlled? When you have a severe fever, what grave consequence may occur if A. destruction of your enzymes' primary structure B. removal of amine groups from your proteins C. change in the tertiary structure of your enzymes D removal of the amino acids in active sites of your enzymes 14.