Overview
Application of fundamental chemistry principles to an understanding of chemical reactions and molecular structure in biological systems.
CHEM 305 Biological and Medicinal Chemistry 2 focuses on more advanced (than CHEM 205) chemical aspects of biological and medicinal systems at a molecular level
The course explores the synthesis of peptides and biological and medicinal peptides, enzyme inhibition and enzyme kinetics at a molecular level, including medicinal chemistry of selected enzyme inhibitors. Chemical aspects of drug discovery and development, including a medicinal chemistry drug discovery laboratory. Application of spectroscopy within biological systems to elucidate biological molecule shape, reactivity and proximity.
About this paper
| Paper title | Biological and Medicinal Chemistry 2 |
|---|---|
| Subject | Chemistry |
| EFTS | 0.15 |
| Points | 18 points |
| Teaching period | Semester 1 (On campus) |
| Domestic Tuition Fees ( NZD ) | $1,243.65 |
| International Tuition Fees | Tuition Fees for international students are elsewhere on this website. |
- Prerequisite
- CHEM 202 or CHEM 205
- Restriction
- PSCI 302
- Recommended Preparation
- CHEM 202 and CHEM 205
- Schedule C
- Science
- Contact
Dr Andrea Vernall
Tel +64 3 479 4518
Location: Science II, 5n4
- Teaching staff
Course Co-ordinator: Dr Andrea Vernall
- Paper Structure
Amino Acids and Peptides
- The chemistry and reactivity of amino acids and peptides.
- Methods of isolation, purification and analysis of peptides and proteins.
- Strategies used in the chemical synthesis of peptides.
- Structure of nucleic acids and role in biological peptide synthesis.
Enzymes
- The role and modes of action of enzymes in catalysing biological reactions.
- Structure activity relationships and kinetics of enzymes.
- Mechanisms of enzyme reactions using proteases as examples.
- Strategies for enzyme inhibition in drug design.
Medicinal compounds – design and optimisation
- Drugs and drug targets at a molecular level, biologically active compounds.
- Physiochemical properties and design features of drugs and chemical tools, including prodrugs and antedrugs, taught via case studies.
- How chemists can rationally design or tune properties of a drug/drug-lead by changing structure.
Spectroscopy of Biological Systems
- FTIR, Raman and FRET spectroscopic techniques to interrogate polypeptides and proteins.
- NMR, EPR and Mossbauer spectroscopy to study specific metalloenzymes
- Teaching Arrangements
- Three lectures per week and one 4-hour lab class per week.
- Textbooks
Recommended:
Jones, J. Amino acid and peptide synthesis, Oxford University Press
Bruice, P.Y. Organic Chemistry, (4th edn), Prentice-Hall
Fersht, A. Enzyme structure and mechanism, Freeman
EBOOK - William O. Foye; Thomas L. Lemke; David A. Williams, Foye’s principles of medicinal chemistry, (7th ed), Wolters Kluwer Health/Lippincott Williams & Wilkins
Graham L. Patrick, An introduction to medicinal chemistry, (5th ed), Oxford Press 2013
- Graduate Attributes Emphasised
Global perspective, Interdisciplinary perspective, Lifelong learning, Scholarship, Ethics, Research, Communication, Critical citizenship, Critical thinking, Information literacy, Self-motivation, Teamwork.
View more information about Otago's graduate attributes.- Learning Outcomes
Expectations at the completion of the paper:
- An understanding of the scientific concepts underlying chemical transformation, structure determination and biological activity of biological molecules.
- An appreciation of the chemical factors controlling biological processes.
- An ability to identify fundamental concepts in chemistry underlying biological systems.
- Demonstrated expertise in the generic activities of information retrieval, critical analysis and presentation, logistical planning and cooperative teamwork.
- An understanding of how chemical knowledge is applied in a practical, problem-solving context.