Laboratory of Biophysical Chemistry
Description of the Group:
Research conducted in the Laboratory of Biophysical Chemistry is focused on cross-roads of chemistry, biology and physics, namely:
- Biological “soft matter”: the relationship between the structure and dynamics of biopolymers (especially proteins) and their macroscopic physicochemical properties, as well as applications of physicochemically modified proteins as new functional bionanomaterials;
- Physicochemical and molecular basis of conformational diseases, aggregation and amyloidogenesis of proteins; the problem of unequivocal encoding of structural information upon amyloid propagation; exotic beta-card structures;
- Non-Anfinsenian behavior of proteins: the conformation memory effect and the phenomenon of chiral bifurcation as examples of highly far-from-equilibrium processes accompanying misfolding of polypeptides and proteins;
- Applications of optical spectroscopy (in particular vibrational spectroscopy and electronic circular dichroism) to study structural transitions of biomacromolecules.
Research Interests:
- Insulin aggregation;
- Protein-solvent interactions;
- Supramolecular chirality of proteins;
- Amyloid;
- Electrostatic interactions in proteins.
Research Equipment:
| Equipment Name | Contact Person / Room Number | |
| 1 | Nicolet iS50 FT-IR spectrometer equipped with a DTGS detector from Thermo Fisher Scientific. | wdzwolak@chem.uw.edu.pl / 1.04 |
| 2 | FLS980 fluorescence spectrometer | wdzwolak@chem.uw.edu.pl / 1.05 |
| 3 | J-815 S spectropolarimeter (CD/ORD) from Jasco | wdzwolak@chem.uw.edu.pl / 1.05 |
Team Leader:
Prof. dr hab. Wojciech Dzwolak graduate of the Faculty of Chemistry of the University of Warsaw (1996 – MSc) and the University of Ritsumeikan in Kyoto (2000 – PhD). Author of over 90 papers in the field of biophysics and physical chemistry of proteins. Laureate of, among others, the 2008 Faculty III Awards of the Polish Academy of Sciences; leader and participant in a number of national and international research projects.
The research conducted by Wojciech Dzwolak (also in cooperation with leading research hubs in Japan, Germany and the USA) focuses on the broadly understood problem of thermodynamic control of self-organizing non-native biopolymer structures.
Key papers:
Puławski W, Dec R, Dzwolak W „Clues to the Design of Aggregation-Resistant Insulin from Proline Scanning of Highly Amyloidogenic Peptides Derived from the N-Terminal Segment of the A-Chain” Mol. Pharm. 21 (2024) 2025–2033.
Dec R, Dzwolak W, Winter R „From a Droplet to a Fibril and from a Fibril to a Droplet: Intertwined Transition Pathways in Highly Dynamic Enzyme-Modulated Peptide-Adenosine Triphosphate Systems” J. Amer. Chem. Soc. 146 (2024) 6045–6052.
Fortunka M, Dec R, Puławski W, Guza M, Dzwolak W “Self-Assembly of Insulin-Derived Chimeric Peptides into Two-Component Amyloid Fibrils: The Role of Coulombic Interactions” J. Phys. Chem. B 127 (2023) 6597-6607.
Dec R, Jaworek M W, Dzwolak W, Winter R „Liquid-Droplet-Mediated ATP-Triggered Amyloidogenic Pathway of Insulin-Derived Chimeric Peptides: Unraveling the Microscopic and Molecular Processes” J. Amer. Chem. Soc. 145 (2023) 4177–4186.
Puławski W, Dzwolak W “Virtual Quasi-2D Intermediates as Building Blocks for Plausible Structural Models of Amyloid Fibrils from Proteins with Complex Topologies: A Case Study of Insulin” Langmuir 38 (2022) 7024–7034.
Wacławska M, Nieznanska H, Dzwolak W „Enzymatic digestion of luminescent albumin-stabilized gold nanoclusters under anaerobic conditions: clues to the quenching mechanism” J. Mater. Chem. C 10 (2022) 3775–3783.
Dec R, Puławski W, Dzwolak W „Selective and stoichiometric incorporation of ATP by self-assembling amyloid fibrils” J. Mater. Chem. B 9 (2021) 8626–8630.
Hernik-Magoń A, Puławski W, Fedorczyk B, Tymecka D, Misicka A, Szymczak P, Dzwolak W „Beware of Cocktails: Chain-Length Bidispersity Triggers Explosive Self-Assembly of Poly-L-Glutamic Acid β2-Fibrils” Biomacromolecules 17 (2016) 1376–1382.
Piejko M, Dec R, Babenko V, Hoang A, Szewczyk M, Mak P, Dzwolak W “Highly Amyloidogenic Two-chain Peptide Fragments Are Released upon Partial Digestion of Insulin with Pepsin” J. Biol. Chem. 290 (2015) 5947–5958.
Surmacz-Chwedoruk W, Nieznańska H, Wójcik S, Dzwolak W, “Cross-Seeding of Fibrils from Two Types of Insulin Induces New Amyloid Strains” Biochemistry 51 (2012) 9460–9469.
Fulara A, Lakhani A, Wójcik S, Nieznaska H, Keiderling TA, Dzwolak W, “Spiral Superstructures of Amyloid-Like Fibrils of Polyglutamic Acid: An Infrared Absorption and Vibrational Circular Dichroism Study” J. Phys. Chem. B 115(2011) 11010–11016.
Loksztejn A, Dzwolak W, “Vortex-Induced Formation of Insulin Amyloid Superstructures Probed by Time-Lapse Atomic Force Microscopy and Circular Dichroism Spectroscopy” J. Mol. Biol. 395 (2010) 643–655.
Dzwolak W, Loksztejn A, Galinska-Rakoczy A, Adachi R, Goto Y, Rupnicki L, “Conformational indeterminism in protein misfolding: chiral amplification on amyloidogenic pathway of insulin” J. Amer. Chem. Soc. 129 (2007) 7517-7522.
Dzwolak W, Ravindra R, Nicolini C, Jansen R, Winter R “The Diastereomeric Assembly of Polylysine Is the Low-Volume Pathway for Preferential Formation of b-Sheet Aggregates” J. Amer. Chem. Soc. 126 (2004) 3762-3768.
Significant Achievement:
The discovery of the phenomenon of chiral bifurcation in the aggregation of insulin consisting in stochastic selection of one of the two types of chiral superstructures of insulin amyloid with different chiraloptical properties. This phenomenon is a unique case of symmetry breaking in molecular biophysics. (Dzwolak et al. J. Amer. Chem. Soc. 129 (2007) 7517-7522)