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Protein identification by 3D OrbiSIMS to facilitate in situ imaging and depth profiling (2020)
Journal Article
Kotowska, A. M., Trindade, G. F., Mendes, P. M., Williams, P. M., Aylott, J. W., Shard, A. G., …Scurr, D. J. (2020). Protein identification by 3D OrbiSIMS to facilitate in situ imaging and depth profiling. Nature Communications, 11(1), Article 5832. https://doi.org/10.1038/s41467-020-19445-x

Label-free protein characterization at surfaces is commonly achieved using digestion and/or matrix application prior to mass spectrometry. We report the assignment of undigested proteins at surfaces in situ using secondary ion mass spectrometry (SIMS... Read More about Protein identification by 3D OrbiSIMS to facilitate in situ imaging and depth profiling.

Evolutionary Drivers of Protein Shape (2019)
Journal Article
Shannon, G., Marples, C. R., Toofanny, R. D., & Williams, P. M. (2019). Evolutionary Drivers of Protein Shape. Scientific Reports, 9(1), Article 11873. https://doi.org/10.1038/s41598-019-47337-8

Diffusional motion within the crowded environment of the cell is known to be crucial to cellular function as it drives the interactions of proteins. However, the relationships between protein diffusion, shape and interaction, and the evolutionary sel... Read More about Evolutionary Drivers of Protein Shape.

Nanofibrous scaffolds support a 3D in vitro permeability model of the human intestinal epitheleum (2019)
Journal Article
Patient, J. D., Hajiali, H., Harris, K., Abrahamsson, B., Tannergreen, C., White, L. J., …Rose, F. R. (2019). Nanofibrous scaffolds support a 3D in vitro permeability model of the human intestinal epitheleum. Frontiers in Pharmacology, 10, Article 456. https://doi.org/10.3389/fphar.2019.00456

Advances in drug research not only depend on high throughput screening to evaluate large numbers of lead compounds but also on the development of in vitro models which can simulate human tissues in terms of drug permeability and functions. Potential... Read More about Nanofibrous scaffolds support a 3D in vitro permeability model of the human intestinal epitheleum.

High-Throughput Miniaturized Screening of Nanoparticle Formation via Inkjet Printing (2018)
Journal Article
Styliari, I. D., Conte, C., Pearce, A. K., Hüsler, A., Cavanagh, R. J., Limo, M. J., Gordhan, D., Nieto-Orellana, A., Suksiriworapong, J., Couturaud, B., Williams, P., Hook, A. L., Alexander, M. R., Garnett, M. C., Alexander, C., Burley, J. C., & Taresco, V. (2018). High-Throughput Miniaturized Screening of Nanoparticle Formation via Inkjet Printing. Macromolecular Materials and Engineering, 303(8), 1-9. https://doi.org/10.1002/mame.201800146

The self‐assembly of specific polymers into well‐defined nanoparticles (NPs) is of great interest to the pharmaceutical industry as the resultant materials can act as drug delivery vehicles. In this work, a high‐throughput method to screen the abilit... Read More about High-Throughput Miniaturized Screening of Nanoparticle Formation via Inkjet Printing.

CRISPR/Cas9 editing in human pluripotent stem cell-cardiomyocytes highlights arrhythmias, hypocontractility, and energy depletion as potential therapeutic targets for hypertrophic cardiomyopathy (2018)
Journal Article
Mosqueira, D., Mannhardt, I., Bhagwan, J. R., Lis-Slimak, K., Katili, P., Scott, E., Hassan, M., Prondzynski, M., Harmer, S. C., Tinker, A., Smith, J. G., Carrier, L., Williams, P. M., Gaffney, D., Eschenhagen, T., Hansen, A., & Denning, C. (2018). CRISPR/Cas9 editing in human pluripotent stem cell-cardiomyocytes highlights arrhythmias, hypocontractility, and energy depletion as potential therapeutic targets for hypertrophic cardiomyopathy. European Heart Journal, 39(43), 3879-3892. https://doi.org/10.1093/eurheartj/ehy249

Aims: Sarcomeric gene mutations frequently underlie hypertrophic cardiomyopathy (HCM), a prevalent and complex condition leading to left ventricle thickening and heart dysfunction. We evaluated isogenic genome-edited human pluripotent stem cell-cardi... Read More about CRISPR/Cas9 editing in human pluripotent stem cell-cardiomyocytes highlights arrhythmias, hypocontractility, and energy depletion as potential therapeutic targets for hypertrophic cardiomyopathy.

Scanning Probe Microscopy, Applications (2016)
Book Chapter
Roberts, C., Davies, M., Tendler, S., & Williams, P. (2017). Scanning Probe Microscopy, Applications. In Encyclopedia of spectroscopy and spectrometry (15-22). (3rd edition). Cham: Elsevier. https://doi.org/10.1016/B978-0-12-803224-4.00275-2

The family of scanning probe microscopes (SPMs) have revolutionary imaging capabilities on a range of materials. For example, atomic resolution images of metal and semiconductor surfaces produced by the scanning tunnelling microscope (STM) or images... Read More about Scanning Probe Microscopy, Applications.

A novel DFP tripeptide motif interacts with the coagulation factor XI apple 2 domain (2016)
Journal Article
Wong, S. S., Østergaard, S., Hall, G., Li, C., Williams, P. M., Stennicke, H., & Emsley, J. (in press). A novel DFP tripeptide motif interacts with the coagulation factor XI apple 2 domain. Blood, 127(23), https://doi.org/10.1182/blood-2015-10-676122

Factor XI (FXI) is the zymogen of FXIa, which cleaves FIX in the intrinsic pathway of coagulation. FXI is known to exist as a dimer and interacts with multiple proteins via its 4 apple domains in the “saucer section” of the enzyme; however, to date,... Read More about A novel DFP tripeptide motif interacts with the coagulation factor XI apple 2 domain.

Monitoring the Dissolution Mechanisms of Amorphous Bicalutamide Solid Dispersions via Real-Time Raman Mapping (2015)
Journal Article

Real-time in situ Raman mapping has been employed to monitor, during dissolution, the crystallization transitions of amorphous bicalutamide formulated as a molecular dispersion in a copovidone VA64 matrix. The dissolution performance was also investi... Read More about Monitoring the Dissolution Mechanisms of Amorphous Bicalutamide Solid Dispersions via Real-Time Raman Mapping.

Multivariate ToF-SIMS image analysis of polymer microarrays and protein adsorption (2015)
Journal Article
Hook, A. L., Williams, P. M., Alexander, M. R., & Scurr, D. J. (2015). Multivariate ToF-SIMS image analysis of polymer microarrays and protein adsorption. Biointerphases, 10, Article 019005. https://doi.org/10.1116/1.4906484

The complexity of hyperspectral time of flight secondary ion mass spectrometry (ToF-SIMS) datasets makes their subsequent analysis and interpretation challenging, and is often an impasse to the identification of trends and differences within large sa... Read More about Multivariate ToF-SIMS image analysis of polymer microarrays and protein adsorption.

Bacterial Attachment to Polymeric Materials Correlates with Molecular Flexibility and Hydrophilicity (2014)
Journal Article
Sanni, O., Chang, C.-Y., Anderson, D. G., Langer, R., Davies, M. C., Williams, P. M., …Hook, A. L. (2015). Bacterial Attachment to Polymeric Materials Correlates with Molecular Flexibility and Hydrophilicity. Advanced Healthcare Materials, 4(5), 695-701. https://doi.org/10.1002/adhm.201400648

A new class of material resistant to bacterial attachment has been discovered that is formed from polyacrylates with hydrocarbon pendant groups. In this study, the relationship between the nature of the hydrocarbon moiety and resistance to bacteria i... Read More about Bacterial Attachment to Polymeric Materials Correlates with Molecular Flexibility and Hydrophilicity.

Atomic force microscopy study of human amylin (20-29) fibrils (2005)
Journal Article
Sedman, V. L., Allen, S., Chan, W. C., Davies, M. C., Roberts, C. J., Tendler, S. J., & Williams, P. M. (2005). Atomic force microscopy study of human amylin (20-29) fibrils. Protein and Peptide Letters, 12(1), 79-83. https://doi.org/10.2174/0929866053406129

Here we present atomic force microscopy images of the fibrils formed by human amylin(20-29). This peptide is a fragment of the polypeptide amylin, the major proteinaceous component of amyloid deposits found in cases of type-II diabetes mellitus. Our... Read More about Atomic force microscopy study of human amylin (20-29) fibrils.