Masha's Biography:

I was born in Moscow, Russia, in 1990. I studied at the Chemistry Department of Lomonosov Moscow State University and received my MSci in 2012.
I then moved to the UK for PhD studies with Prof Richard Hartley (University of Glasgow) and Prof Mike Murphy (University of Cambridge). There, I worked on small molecule tools to study oxidative stress in mitochondria, and received my PhD in 2017.
I then changed fields (and cities) and joined the groups of Prof Ed Tate and Prof Aylin Hanyaloglu at Imperial College London to work on G protein-coupled receptors (GPCRs). My research focused on the development of novel chemogenetic and proximity proteomics approaches to study GPCR function.

Combining my training in several different fields - redox biology, GPCR chemical biology and proteomics - I am now leading the GPCR chemical biology and proteomics group at the University of Bath. We work on developing new proteomics approaches and small molecule tools for GPCRs and study how GPCR signalling is affected by oxidative stress-related conditions in disease.

Outside the lab, I am a mom of two little girls. In my spare time (speaking rhetorically), I am a fan of painting, reading, and hiking some challenging terrains (the GR20 trail is my favourite so far).

Research Interests:

Our research is highly multidisciplinary and we are always looking for fruitful collaborations. If you are interested in what we are doing, please contact Masha directly.

Our research group is based on three pillars - chemistry, molecular biology and proteomics. Our overall goal is to develop high-precision chemical biology approaches to interrogate dynamic protein interactions, contributing to understanding the molecular mechanisms of disease and promoting new drug discovery.

We are particularly interested in deciphering the roles of G protein-coupled receptors (GPCRs) in the development of disease. GPCRs are the superfamily of membranes proteins and highly popular drug targets.

Our current projects are:

i) APEX2 proximity proteomics technology.
We develop proximity proteomics technologies to resolve GPCR interactomes and find new potentially druggable protein interactions. APEX2 proximity proteomics is an emerging and powerful approach to resolve protein interaction networks in both time and space, directly in live cells. In this approach, the protein of interest is genetically fused with a small APEX2 tag, an engineered ascorbate peroxidase. The interactome of the protein of interest in ~20 nm proximity to the target is then biotinylated, enriched and coupled to quantitative mass spectrometry proteomics, followed by interactomics data analysis. For an example of the APEX2 technology applied to a GPCR for luteinizing hormone, LHR, please refer to our latest paper published in Cell Chem Bio 2025.
At the moment, we are focused on deciphering interactomes of the metabolic receptors, such as GCGR, GIPR and GPR119.

ii) Dissecting the link between lipid peroxidation and GPCR function in type 2 diabetes.
GPCRs are highly-attractive drug targets in type 2 diabetes (T2D) and other metabolic disorders (think of a popular Ozempic targeting GLP-1 receptor). However, many more promising drugs do not work in patients. We are interested to understand why.
Lipid peroxidation (LPO) in cell membranes contributes to progression of T2D. It generates reactive aldehydes as end-products, and these are highly reactive electrophiles. They form irreversible adducts with proteins in a process called carbonylation.
Carbonylation significantly modulates protein function, signalling and interactions. Importantly, reactive aldehydes are produced in cell membranes, right where GPCRs sit…
We are particularly interested to investigate what happens to metabolic GPCRs when they are attacked by reactive aldehydes, and how this regulates their function. This process potentially has significant implications in how GPCRs respond to their drugs and interact with other proteins in T2D and other metabolic disorders.
Through systemic studies, we are looking at various levels of GPCR regulation by reactive aldehydes derived from LPO.

At the moment, our focus is on three metabolic GPCRs, GCGR, GIPR and GPR119.

• Using APEX2 proximity proteomics, we investigate how LPO affects GPCR interactions.
• Using chemoproteomics, we search for and map carbonylation sites on GPCRs.
• Using cell signalling assays and confocal microscopy, we investigate how LPO affects GPCR downstream signalling and trafficking.

iii) High-precision chemical tools to study GPCRs.
We work on light-responsive drugs that can activate GPCRs of interest on demand with a short pulse of light, followed by functional assessment in intact cells. We develop bivalent antibody-drug conjugates that can target GPCRs of interest in a cell-specific manner (for example, target GPCRs expressed on cancer cells vs healthy cells).