- Bilkent University, Ankara, Turkey B.Sc. in Chemistry, 2005
- Max Planck Institute (MPIP), Mainz, Germany Ph.D. in Solid-state NMR, 2008
- Leibniz Institute for Molecular Pharmacology (FMP), Berlin, Germany Postdoctoral Associate in Structural Biology, 2009-2015
- Aarhus University (iNano - AIAS), Aarhus, Denmark Assistant Professor, 2015 - 2018
- Forschung Zentrum Julich (FZJ), Julich, Germany Senior Scientist, 2018-2019
- Weizmann Institute of Science, Rehovot, Israel Senior Scientist, 2020-2021
- Radboud University of Science, Nijmegen, The Netherlands Senior Scientist, 2021
Education & Training
Chang-Hyeock Byeon, Pang C. Wang, In-Ja L. Byeon, Ümit Akbey. (2023) Solution-state NMR assignment and secondary structure propensity of the full length and minimalistic-truncated prefibrillar monomeric form of biofilm forming functional amyloid FapC from Pseudomonas aeruginosa. Biomolecular NMR Assign.
Chang-Hyeock Byeon, Ümit Akbey. (2023) Solution-state NMR assignment and secondary structure analysis of the monomeric Pseudomonas biofilm-forming functional amyloid accessory protein FapA. Biomolecular NMR Assign.
Ümit Akbey. (2023) Site-specific Protein Methyl Deuterium Quadrupolar Patterns by Proton detected 3D 2H13C1H MAS NMR Spectroscopy. Solid State Nuclear Magnetic Resonance, 125, 101861.
Ümit Akbey, Maria Andreasen. (2022). Functional amyloids from bacterial biofilms - structural properties and interaction partners. Invited Review. Chemical Science, 13(22), 6457-6477.
Ümit Akbey. (2022) Site-specific Protein Methyl Deuterium Quadrupolar Patterns by Proton detected 3D 2H13C1H MAS NMR Spectroscopy. Journal of Biological NMR. 76, 23–28.
Ümit Akbey. (2021) Dynamics of uniformly labelled solid proteins between 100 and 300 K: A 2D 2H13C MAS NMR approach. Journal of Magnetic Resonance, 327, 106974.
Nelson Ferreira, Emil Gregersen, Zachary A. Sorrentino, Hjalte Gram, Cristine Betzer, Clara Perez-Gozalbo, Marjo Beltoja, Madhu Nagaraj, Jie Wang, Jan S. Nowak, Mingdong Dong, Daniel Otzen, Ümit Akbey, Sissel Schmidt, Morten Meyer, Marina Romero-Ramos, Benoit Giasson, Poul H. Jensen. (2021) Multiple system atrophy-associated oligodendroglial protein p25 alpha stimulates formation of novel alpha-synuclein strain with enhanced neurodegenerative potential. Acta Neuropathologica 142, 1, 87-115.
Madhu Nagaraj; Mumdooh Ahmed; Jeppe Lyngso; Brian S. Vad; Andreas Bogglid; Anne Filipsen; Jan Skov Pederson; Daniel Otzen, Ümit Akbey. (2020) Predicted Loop Regions Promote Aggregation: A Study of Amyloidogenic Domains in the Functional Amyloid FapC. Journal of Molecular Biology 432, 7, 2232-2252.
Anne Diehl, Yvette Roske , Linda Ball , Anup Chowdhury , Mattias Hiller , Noel Moliere , Regina Kramer, Daniel Stöppler , Catherine L. Worth , Brigitte Schlegel , Martina Leidert , Nils Cremer , Natalja Erdmann , Daniel Lopez , Heike Stephanowitz , Eberhard Krause , Barth-Jan van Rossum , Peter Schmieder , Udo Heinemann , Kursad Turgay , Ümit Akbey, Hartmut Oschkinat. (2018) Structural changes of TasA in biofilm formation of Bacillus. PNAS, 27, 115 (13), 3237-3242.
Ümit Akbey and Hartmut Oschkinat (2016) Structural Biology Applications of Solid State MAS DNP NMR Journal of Magnetic Resonance 269, 213-224.
Ümit Akbey, Andrew J. Nieuwkoop, Sebastian Wegner, Anja Voreck, Britta Kunert, Priyanga Bandara, Frank Engelke, Niels Chr. Nielsen, Hartmut Oschkinat. (2014) Quadruple-Resonance MAS NMR Spectroscopy of Deuterated Solid Proteins. Angew. Chem. Int. Ed. 53, 2438-2442.
The Akbey Lab use modern solid state NMR (ssNMR) spectroscopy to study biofilm forming functional bacterial amyloid (FuBA) fibrils. Moreover, we have interest in pathologic amyloid fibrils causing neurodegenerative diseases. We develop novel ssNMR methods to push the limits of the state of the art and apply these methods to understand molecular details and mechanisms of insoluble and non-crystalline proteins. Solid-state NMR has made a remarkable progress in the last decade to become a high-resolution and -sensitivity method due to advances in sample preparation, hardware, novel methods such as proton-detection and hyperpolarization (DNP). These allow studies of not only difficult proteins in-vitro, but also in their complex in-vivo environment. We also like to combine ssNMR with other exciting structural biology tools, such as electron microcopy (EM). We use recombinant protein expression and biophysical methods to produce and characterize isotope labeled protein samples.
Our functional amyloid systems are a unique class of amyloid fibrils with specific biological functions in living organisms, in contrast to the pathologic amyloids causing disease. A subgroup of these systems is biofilm forming bacterial functional amyloids (FuBA), a major cause of persistent infections and an antimicrobial resistance (AMR) target. We focus on the NMR-based structural biology of these functional amyloids. We aim to determine atomic resolution structure and molecular dynamics information, for better understanding of amyloid formation, biofilms, and their interactions. This will pave the way towards future treatments against bacterial infections and their antimicrobial resistance.
University of Pittsburgh & UPMC Competitive Medical Research Fund (CMRF), 2023-2025
Research Infrastructure Access Grant, iNext Discovery, European Union, 2022-2024