Postgraduate Course: Quantitating Drug Binding (BICH11011)
Course Outline
| School | School of Biological Sciences |
College | College of Science and Engineering |
| Credit level (Normal year taken) | SCQF Level 11 (Postgraduate) |
Availability | Not available to visiting students |
| SCQF Credits | 20 |
ECTS Credits | 10 |
| Summary | Introduce the core ideas and importance of determining, using various biophysical techniques, a drug:target affinity. Using practical sessions and workshops, students will be introduced to an industry standard technique for determining a Kd. They will also be introduced to a number of other biophysical platforms for determining binding constants and these will be discussed and considered, along with other less applicable, lower throughout platforms, with an emphasis on the appropriate windows in which they can be applied. |
| Course description |
Introduce the core ideas and importance of determining, using various biophysical techniques, a drug:target affinity. Practical lab sessions, will allow students to determine the equilibrium binding constant of a small SAR family of drug molecules, and a competitive inhibitor, to Human Serum Albumen (HSA) using a modern, industry standard fluorescence polarisation (utilised as primary, secondary and tertiary analysis platform in the pipeline) using a multi-mode UV-Vis fluorimeter platform. Further sessions will derive the binding constants, fractional occupancy and Kiapp, using linear and non-linear transformations to further describe/determine parameters like stoichiometry and active site number. This analysis will lead to a critical examination of the design of the experiment and the general application of affinity determination in the drug discovery pipeline and the basic concept of an SARs. Other standard techniquesfor determining binding constants will be discussed and considered, along with other less applicable, lower throughout platforms, with an emphasis on the appropriate windows in which they can be applied and potential artefacts and pitfalls.
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Entry Requirements (not applicable to Visiting Students)
| Pre-requisites |
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Co-requisites | |
| Prohibited Combinations | |
Other requirements | None |
Course Delivery Information
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| Academic year 2026/27, Not available to visiting students (SS1)
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Quota: 24 |
| Course Start |
Semester 1 |
Timetable |
Timetable |
| Learning and Teaching activities (Further Info) |
Total Hours:
200
(
Lecture Hours 8,
Seminar/Tutorial Hours 15,
Supervised Practical/Workshop/Studio Hours 16,
Summative Assessment Hours 6,
Programme Level Learning and Teaching Hours 4,
Directed Learning and Independent Learning Hours
151 )
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| Assessment (Further Info) |
Written Exam
0 %,
Coursework
100 %,
Practical Exam
0 %
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| Additional Information (Assessment) |
ICA 1 (30%): Presentation session on alternative biophysical technique for determining drug:target affinity/binding.
ICA 2 (70%): Extended practical lab report. Detailed report with analysis, in the style of a research paper. |
| Feedback |
ICA 1: Feedback provided in presentation feedback session.
ICA 2: Written feedback provided. |
| No Exam Information |
Learning Outcomes
On completion of this course, the student will be able to:
- Acquire a deeper knowledge and critical appreciation of how binding constants for drug molecules to their targets are determined, with specific focus on FP, an industrial standard for the initial (and sometimes later) stages of a drug discovery pipeline/programme.
- Be competent to carry out the experimental manipulations to determine a binding constant of a small series of drugs, and a direct competitor, to its target using a modern binding assay.
- Understand how to derive a binding constant of a drug to its target and the stoichiometry from experimental data.
- Apply various binding models to direct and competition data, and understand the variances, limitations and errors in the data/platform and critically comment on them and suggest alternative methodologies/platforms for orthogonal analysis.
- Find references and read into an academic subject given a starter reference, and develop presentation and group-working skills around the contextual starting material.
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Additional Information
| Graduate Attributes and Skills |
Knowledge/understanding: lectures provide the frame-work for development of core ideas around what an affinity constant is and why it is one of the critical parameters in a drug/translational discovery project or industrial pipeline. Content is delivered by staff with an international track record of designing and implementing the biochemical/biophysical themes in drug-discovery programmes, both in the academic setting and for Biopharma.
Research communication and understanding: skills enhancement with a view to development of own experimental design and data (own and published) interpretation, by further reading; papers, appreciate review, best practice industrial SOPs. This will build on the core theory and help develop a critical analysis, through oral and written assessments that allow appreciation for variances, limitations and errors in the data/platform and critically comment on them and suggest alternative methodologies/platforms for orthogonal analysis. Opportunity for development of effective communication skills and peer feedback.
Technical competency and laboratory skills: students will develop transferable laboratory skills, in an analytical environment as well as enhancing data handling and numeracy. All are important for progression on other Semester-2 and particular semester-2 courses, developing focussed research skills, as well as an understanding of the environmental, health and social
problems that accompany work in the field of drug discovery and working with proteins and their ligands. This will provide individuals capable of pursuing a professional career in industry or government agencies or continuing their research at PhD level. |
| Keywords | Not entered |
Contacts
| Course organiser | Dr Martin Wear
Tel: (0131 6)50 7054
Email: Martin.Wear@ed.ac.uk |
Course secretary | Ms Louise Robertson
Tel: (0131 6)50 8649
Email: Louise.K.M.Robertson@ed.ac.uk |
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