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DEGREE REGULATIONS & PROGRAMMES OF STUDY 2021/2022

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DRPS : Course Catalogue : School of Biological Sciences : Postgraduate

Postgraduate Course: Detailed Characterisation of Drug or Ligand Interactions Using Surface Plasmon Resonance (SPR) (BILG11005)

Course Outline
SchoolSchool of Biological Sciences CollegeCollege of Science and Engineering
Credit level (Normal year taken)SCQF Level 11 (Postgraduate) AvailabilityNot available to visiting students
SCQF Credits10 ECTS Credits5
SummaryThis course will discuss the practical use of Surface Plasmon Resonance to characterise biophysical interactions, and will show how the affinity, kinetic and thermodynamic data generated from such experiments can be used to enrich and accelerate the progress of accurate SARs in the development of drugs and therapeutics. The data handling and processing of affinity/kinetic and thermodynamic data will be applicable to other biophysical characterisation techniques.
Course description Theoretical background of SPR.
Practical instrumental and experimental considerations for surface and data generation with small molecules and fragments.
Thermodynamic profiling
Data analysis - kinetic, affinity and thermodynamic.
Use of SPR data for small molecule:protein SARs.

Surface plasmon resonance (SPR) is routinely exploited in the kinetic analysis of biomolecular interactions and small-molecule drug-discovery/hit-validation studies. SPR instruments uniquely allow the measurement of kinetic and thermodynamic data specifically associated with complex formation and dissociation. Such SPR data can be used to "thermodynamic profile" interactions enhancing the correlation of solution binding measurements with structural features and the assignment of proportional energetic contributions to individual functional groups, the basis of the whole-structure-based design approach to engineered therapeutics and drug design. This course will provide both theoretical and some hands on-experience of the practical use of SPR to characterise biophysical interactions, and will show how the affinity, kinetic and thermodynamic data generated from such experiments can be used to enrich and accelerate the progress of accurate SARs in the development of drugs and therapeutics. The data handling and processing of affinity/kinetic and thermodynamic data will be applicable to other biophysical characterisation techniques.
Entry Requirements (not applicable to Visiting Students)
Pre-requisites Co-requisites
Prohibited Combinations Other requirements None
Additional Costs 0
Course Delivery Information
Academic year 2021/22, Not available to visiting students (SS1) Quota:  36
Course Start Semester 2
Timetable Timetable
Learning and Teaching activities (Further Info) Total Hours: 100 ( Lecture Hours 30, Programme Level Learning and Teaching Hours 2, Directed Learning and Independent Learning Hours 68 )
Assessment (Further Info) Written Exam 0 %, Coursework 100 %, Practical Exam 0 %
Additional Information (Assessment) In Course Assessment - 100%

An ICA consisting of a data analysis of an example dataset of affinity, kinetic and thermodynamic data and generation of report describing development of further experiments/considerations for development of the theoretical drug/therapeutic based on the SARs generated/supplied.
Feedback Verbal feedback will be provided throughout the course. Written feedback will be provided on the written assessment at the end of the course.
No Exam Information
Learning Outcomes
On completion of this course, the student will be able to:
  1. Demonstrate an understanding of the technologies that underpin SPR instruments and experiments.
  2. Demonstrate the ability to successfully generate and analyse an example dataset of affinity, kinetic and thermodynamic data.
  3. Discuss their results in a relation to the basic SARs of a model example protein:small molecule system.
  4. llustrate an understanding of the interplay between, affinity, stability, kinetics and thermodynamics in relation to protein:ligand interactions.
  5. Analyse SPR data sets and rationalise the effect of temperature on the kinetics and then extrapolate this to a 'thermodynamic profile' of the protein:ligand interaction.
Reading List
N/A
Additional Information
Graduate Attributes and Skills Understanding of Surface plasmon resonance and its uses
Special Arrangements N/A
Study Abroad N/A
KeywordsSPR
Contacts
Course organiserDr Martin Wear
Tel: (0131 6)50 7054
Email: Martin.Wear@ed.ac.uk
Course secretaryMrs Claire Black
Tel: (0131 6)50 8637
Email: Claire.Black@ed.ac.uk
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