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Mapping the Folding and Assembly Landscapes of Amyloidogenic Peptides


   Department of Chemistry

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  Dr A Borysik, Dr M Ulmschneider  No more applications being accepted  Competition Funded PhD Project (Students Worldwide)

About the Project

The aggregation of unstructured amyloidogenic peptides is implicated in a number a diseases including Alzheimer’s and Creutzfeldt-Jakob disease. In isolation, amyloidogenic peptides are characterised by the absence of a defined 3-dimensional conformation, but adoption of structurally ordered assemblies is associated with pathogenesis, in a process that is poorly understood. Ordered peptide assemblies have been shown to interact with biological membranes promoting pore formation, membrane penetration and cell death. Understanding the molecular mechanisms orchestrating the disorder-to-order transition and self-assembly of amyloidogenic peptides provides an opportunity for the design of new therapeutics to prevent disease. The characterisation of these early disease forming events represents a significant challenge, however, due to the unstructured nature of the peptide monomers, which thwarts exploration via established structural techniques. It is not known, for example, if the transition to order requires a transient template within each peptide monomer or if structure emerges as a consequence of self-assembly or lipid binding.

This project will entail the development of new methods to characterise the folding and assembly landscape of amyloidogenic peptides. The ability to pinpoint amino acids that are critical for peptide aggregation and the characterisation of transient structure within the unfolded ensembles will provide a new blueprint to understand peptide misfolding disorders. The method will sit at the interface between biophysics and computational biology with the student developing and applying in silico methods to define the unstructured peptide ensemble and identify amino acids critical for peptide assembly.1-2 The computational methods will be corroborated by state-of-the-art experimental techniques developed by the Borysik group that can quantify the degree of disorder in biomolecules with amino acids resolution.3-4 The project will be complimented by a range of biochemical and membrane assays aimed to unearth the foremost molecular events in peptide misfolding disorders.

For informal enquires email: antoni.borysik(@)kcl.ac.uk , martin.ulmschneider(@)kcl.ac.uk

Group site: www.kcl.ac.uk/people/antoni-borysik, www.kcl.ac.uk/people/martin-ulmschneider

Application Procedure

Send your CV and a research statement to: PGR-chemistry(@)kcl.ac.uk

Your research statement must detail:

  1. Your previous research experience (final year projects, summer placements, year in industry etc).
  2. Why you want to do a PhD and why you chose this programme

Complete an online application on the King’s College myApplication system at apply.kcl.ac.uk/

  1. Register a new account/login
  2. Once logged in, select Create a new application
  3. Enter ‘Chemistry Research MPhil/PhD (Full-time/Part-time)' under Choose a programme. Please ensure you select the correct mode of study.

CV submission and online application MUST both be completed by the deadline.

At King’s, we are deeply committed to embedding good equality and diversity practice into all of our activities so that the university is an inclusive, welcoming and inspiring place to study, regardless of age, disability, gender reassignment, marital status, pregnancy and maternity, race, religion, sex or sexual orientation.

This position is now open to international Students.


Funding Notes

The studentships are funded for 4 years, with a stipend at the standard research council rate, which is presently £17,609 per annum including London Allowance, and cover the full cost of Home tuition fees. Income tax is not payable on the stipend.

References

[1] C. H. Chen et al. J. Amer. Chem. Soc. 2019, 141, 12, 4839-4848.
[2] J. P. Ulmschneider & M. B. Ulmschneider. Accounts of Chemical Research 2018, 51 (5), 1106-1116
[3] R. E. Salmas and A. J. Borysik Commun Bio 2021, 4, 199
[4] R. E. Salmas and A. J. Borysik Anal Chem 2021, 93, 7323
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