PhD - Decoding protein aggregation in neurodegenerative diseases using advanced mass spectrometry methods

University of Leeds, United Kingdom; Leeds; On-site; GBP 20,000 - 24,000; Full time

Job summary

University of Leeds in the United Kingdom invites applications for a PhD project focussed on decoding protein aggregation in neurodegenerative diseases using advanced mass spectrometry methods. The project will explore TDP-43 and α-synuclein, leveraging state-of-the-art MS and hydrogen–deuterium exchange MS to characterise structural transitions from soluble proteins to oligomers and amyloid fibrils.

Working in partnership with Waters Corporation, the student will gain access to cutting-edge

Qualifications

• Enrolled or eligible for PhD studies in chemistry, biochemistry or related field.
• Strong data analysis and experimental design skills.
• Experience with mass spectrometry is desirable.

Responsibilities

• Characterise protein aggregation using MS and HDX-MS techniques.
• Collaborate with Waters Corporation to access state-of-the-art instrumentation.
• Develop and apply advanced MS methods to study protein misfolding in neurodegenerative diseases.

Skills

Mass spectrometry

HDX-MS

Structural biology

Education

PhD in Chemistry/Biochemistry/Biology

Tools

HDX-MS instrumentation

Waters mass spectrometers

Job description

Jobs in Structural Biology and Related Fields

PhD - Decoding protein aggregation in neurodegenerative diseases using advanced mass spectrometry methods

University of Leeds, United Kingdom

Neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and Parkinson's disease (PD) are characterised by the misfolding and aggregation of proteins into toxic assemblies that damage neurons. However, the molecular events that convert functional proteins into disease-causing aggregates and amyloid fibrils remain poorly understood.

This PhD project will investigate two proteins central to these disorders: TDP-43, the pathological hallmark of most ALS and many FTD cases, and α-synuclein, the major component of Lewy bodies in PD. Both proteins can transition between soluble states, biomolecular condensates, oligomers, and amyloid fibrils. Understanding how and why these transitions occur is a key challenge hampering the development of new therapeutic strategies.

The project will use and develop state-of-the-art mass spectrometry (MS) approaches to characterise the structural changes that occur during protein aggregation. Working in partnership with Waters Corporation, a global leader in analytical technologies, you will gain access to cutting-edge instrumentation while developing next-generation hydrogen-deuterium exchange mass spectrometry (HDX-MS) methods.

This highly interdisciplinary project sits at the interface of analytical chemistry, structural biology, and neuroscience. It offers comprehensive training in advanced mass spectrometry, protein biochemistry, data analysis, and scientific communication, while providing experience in both academic and industrial research environments. The outcomes will advance our understanding of neurodegenerative disease and deliver innovative technologies with broad applications across biomedical research and drug discovery.

For informal enquiries about the project, please contact Dr Antonio Calabrese, Associate Professor, School of Molecular and Cellular Biology [e-mail]

Application deadline: 5pm (GMT), Wednesday 6th January 2027