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 ) | $1,318.20 |
| 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.
- Physiocochemical 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.
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 | Tuition Fees for 2027 have not yet been set |
| 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
- Dr Nick Green
- Dr Eng Wui Tan
- Dr Courtney Ennis
- 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.
- Physicochemical 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. (2002). Amino Acid and Peptide Synthesis (2nd ed.). Oxford University Press.
Bruice, P. Y. (2020). Organic Chemistry (8th ed.). Pearson.
Fersht, A. (1985). Enzyme structure and mechanism (2nd ed.). Freeman.
Lemke, T. L., Roche, V. F., & Fore, W. O. (2013). Foye’s principles of medicinal chemistry (7th ed.). Wolters Kluwer Health/Lippincott Williams & Wilkins.
Patrick, G. L. (2013). An introduction to medicinal chemistry (5th ed.). Oxford Press.- Graduate Attributes Emphasised
- Interdisciplinary perspective, Lifelong learning, Scholarship, Communication, Critical thinking, Ethics, Information literacy, Research, Self-motivation, Teamwork.
View more information about Otago's graduate attributes. - Learning Outcomes
Students who successfully complete this paper will be expected to have:
- 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.