Gabriella (Gabi) Heller is the Rosalind Franklin Research Fellow at Newnham College. Her research focuses on intrinsically disordered proteins, biomolecules lacking a single, rigid three-dimensional structure that instead exist as a dynamic equilibrium of conformationally distinct states. These proteins are highly prevalent in diseases such as dementia and cancer, yet are often considered therapeutically 'untargetable' as they are unamenable to traditional drug discovery techniques. Gabriella aims to understand whether and how intrinsically disordered proteins can be targeted by small molecule therapeutics using a combination of computational and experimental techniques.
Publications
A small molecule stabilises the disordered native state of the Alzheimer’s Aβ peptide
(2021)
2021.11.10.468059
(DOI: 10.1101/2021.11.10.468059)
Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer's disease
– Sci Adv
(2020)
6,
eabb5924
(DOI: 10.1126/SCIADV.ABB5924)
Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors.
– Proceedings of the National Academy of Sciences
(2020)
117,
24251
(DOI: 10.1073/pnas.2006684117)
Rational design of a conformation-specific antibody for the quantification of Aβ oligomers.
– Proceedings of the National Academy of Sciences of the United States of America
(2020)
117,
13509
(DOI: 10.1073/pnas.1919464117)
A kinetic ensemble of the Alzheimer’s Aβ peptide
(2020)
2020.05.07.082818
(DOI: 10.1101/2020.05.07.082818)
Small molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer’s disease
(2019)
729392
(DOI: 10.1101/729392)
Promoting transparency and reproducibility in enhanced molecular simulations
– Nat Methods
(2019)
16,
670
(DOI: 10.1038/s41592-019-0506-8)
Determination of Structural Ensembles of Proteins: Restraining vs Reweighting.
– Journal of Chemical Theory and Computation
(2018)
14,
6632
(DOI: 10.1021/acs.jctc.8b00738)
Structural Ensemble Modulation upon Small-Molecule Binding to Disordered Proteins
– J Mol Biol
(2018)
430,
2288
(DOI: 10.1016/j.jmb.2018.03.015)
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