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Dek Woolfson

Professor

University of Bristol

Talk Information

Peptide Materials

16 June 2025, 04:10pm - 04:40pm, in the Pacific Jewel Ballroom
L17 - AWFrom Peptides to Proteins to Functions by Design

Dek Woolfson

Award Recipient

2025 du Vigneaud Award
The Vincent du Vigneaud Awards recognize outstanding achievement in peptide research at mid-career. The du Vigneaud Awards are sponsored by Bachem, and are awarded to two deserving recipients at the biennial American Peptide Symposia.



Professor Dek N. Woolfson holds a joint appointment in the Schools of Chemistry and Biochemistry at the University of Bristol. He is also the Director of the Bristol BioDesign Institute and a founding director of the Max Planck-Bristol Centre for Minimal Biology. His research focuses on the rational design of novel protein structures and assemblies, bridging the disciplines of chemistry, biology, and synthetic biology.

Academic Background

Professor Woolfson earned his B.A. in Chemistry from the University of Oxford in 1987, conducting undergraduate research with Professor Christopher M. Dobson. He completed his Ph.D. in Chemistry and Biochemistry at the University of Cambridge in 1991 under the supervision of Professor D.H. Williams and Dr. P.A. Evans. Following postdoctoral research at University College London and the University of California, Berkeley, he held academic positions at the University of Sussex before joining the University of Bristol in 2005.

Research Focus

Professor Woolfson's laboratory specializes in de novo protein design, aiming to create entirely new protein structures not found in nature. His team employs computational and experimental approaches to design coiled-coil proteins, peptide assemblies, and synthetic biomaterials. These designed proteins have applications in understanding fundamental aspects of protein folding, as well as in developing novel biomaterials and therapeutic agents.

Notable Contributions

Professor Woolfson has made significant contributions to the field of protein design, including the development of computational tools for modeling coiled-coil structures and the creation of self-assembling peptide-based materials. His work has been recognized with several awards, such as the Medimmune Protein and Peptide Science Award, 2011, the Royal Society Wolfson Research Merit Award, 2014, the Interdisciplinary Prize of the Royal Society of Chemistry, 2016, and the Humboldt Research Award, 2020.

Professional Engagements

Beyond his research, Professor Woolfson is actively involved in mentoring and teaching, supervising numerous graduate students and postdoctoral researchers. He is also the founder of Rosa Biotech, a spin-out company focused on developing biosensing technologies based on synthetic protein scaffolds.

Through his innovative research and leadership in synthetic biology, Professor Dek N. Woolfson continues to advance the frontiers of protein design and its applications in science and medicine.



From Peptides to Proteins to Functions by Design

Dek Woolfson

Schools of Chemistry and Biochemistry, & Bristol BioDesign Institute, University of Bristol, UK

It is now possible to generate many stable peptide assemblies and proteins from scratch using rational and computational design approaches. One challenge in this field of de novo protein design is to move past structures found in nature and target the ‘dark matter of protein space’; that is, structures that should be possible in terms of chemistry and physics, but which biology seems to have overlooked. This talk will illustrate what is currently possible in this nascent area using de novo designed coiled-coil peptides and proteins.

I will describe our “toolkit” of de novo coiled-coil assemblies (1), and how we are converting these peptides bundles and barrels into single-chain proteins through rationally seeded computational protein design (2). Then I will turn to subcellular applications. I will describe new designs and systems including (i) de novo cell-penetrating peptides (3), and (ii) high-affinity kinesin-binding peptides (4), and how these can be combined to hijack and control active motor proteins in living cells (5).

(1) Understanding a protein fold: The physics, chemistry, and biology of alpha-helical coiled coils
DN Woolfson
J Biol Chem 299, ARTN: 104579 (2023). DOI: 10.1016/j.jbc.2023.104579

(2) Rationally seeded computational protein design of α-helical barrels
KI Albanese, R Petrenas, F Pirro, EA Naudin, U Borucu, WM Dawson, DA Scott, GJ Leggett, OD Weiner, TAA Oliver, DN Woolfson
Nat Chem Biol 20, 991–9 (2024). DOI: 10.1038/s41589-024-01642-0

(3) De novo designed peptides for cellular delivery and subcellular localisation
GG Rhys, JA Cross, WM Dawson, HF Thompson, S Shanmugaratnam, NJ Savery, MP Dodding, B Höcker, DN Woolfson
Nat Chem Biol 18, 999– (2022). DOI: 10.1038/s41589-022-01076-6

(4) Fragment-linking peptide design yields a high-affinity ligand for microtubule-based transport
JA Cross, MS Chegkazi, RA Steiner, DN Woolfson, MP Dodding
Cell Chem Biol 28, 1347–1355 (2021). DOI: 10.1016/j.chembiol.2021.03.010

(5) A de novo designed coiled coil-based switch regulates the microtubule motor kinesin-1
JA Cross, WM Dawson, SR Shukla, JF Weijman, J Mantell, MP Dodding, DN Woolfson
Nat Chem Biol 20, 916–23 (2024). DOI: 10.1038/s41589-024-01640-2