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Structure and dynamics of monoclonal antibody domains determined using spins, scattering, and simulations.
ChemMedChem
January 2025
National Institute of Standards and Technology, Material Measurement Laboratory, UNITED STATES OF AMERICA.
Antibody-based pharmaceuticals are the leading biologic drug platform (> $75B/year). Despite a wealth of information collected on them, there is still a lack of knowledge on their inter-domain structural distributions, which impedes innovation and development. To address this measurement gap, we have developed a new methodology to derive biomolecular structure ensembles from distance distribution measurements via a library of tagged proteins bound to an unlabeled and otherwise unmodified target biologic.
View Article and Find Full Text PDFComparison of lipid dynamics and permeability in styrene-maleic acid and diisobutylene-maleic acid copolymer lipid nanodiscs by electron paramagnetic resonance spectroscopy.
J Biol Inorg Chem
January 2025
Department of Chemistry and Biochemistry, Miami University, Oxford, OH, USA.
Lipid nanoparticles formed with copolymers are a new and increasingly powerful tool for studying membrane proteins, but the extent to which these systems affect the physical properties of the membrane is not completely understood. This is critical to understanding the caveats of these new systems and screening for structural and functional artifacts that might be caused in the membrane proteins they are used to study. To better understand these potential effects, the fluid properties of dipalmitoylphosphatidylcholine lipid bilayers were examined by electron paramagnetic resonance (EPR) spectroscopy with spin-labeled reporter lipids in either liposomes or incorporated into nanoparticles with the copolymers diisobutylene-maleic acid or styrene maleic acid.
View Article and Find Full Text PDFNanoclusters of Guest Molecules in Lipid Rafts of a Model Membrane Revealed by Pulsed Dipolar EPR Spectroscopy.
J Phys Chem B
January 2025
Institute of Chemical Kinetics and Combustion, Russian Academy of Sciences, Novosibirsk 630090, Russia.
Plasma membranes are known to segregate into liquid disordered and ordered nanoscale phases, the latter being called lipid rafts. The structure, lipid composition, and function of lipid rafts have been the subject of numerous studies using a variety of experimental and computational methods. Double electron-electron resonance (DEER, also known as PELDOR) is a member of the pulsed dipole EPR spectroscopy (PDS) family of techniques, allowing the study of nanoscale distances between spin-labeled molecules.
View Article and Find Full Text PDFInsights into Folding and Molecular Environment of Lyophilized Proteins Using Pulsed Electron Paramagnetic Resonance Spectroscopy.
Mol Pharm
January 2025
Pharmaceutical Technology and Biopharmaceutics, Department of Pharmacy, Ludwig-Maximilians-Universität München, Butenandtstrasse 5-13, 81377 Munich, Germany.
There is still an insufficient understanding of how the characteristics of protein drugs are maintained in the solid state of lyophilizates, including aspects such as protein distances, local environment, and structural preservation. To this end, we evaluated protein folding and the molecules' nearest environment by electron paramagnetic resonance (EPR) spectroscopy. Double electron-electron resonance (DEER) probe distances of up to approximately 200 Å and is suitable to investigate protein folding, local concentration, and aggregation, whereas electron spin echo envelope modulation (ESEEM) allows the study of the near environment within approximately 10 Å of the spin label.
View Article and Find Full Text PDFFrequency and time domain F ENDOR spectroscopy: role of nuclear dipolar couplings to determine distance distributions.
Phys Chem Chem Phys
January 2025
Research Group ESR Spectroscopy, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, Göttingen, Germany.
F electron-nuclear double resonance (ENDOR) spectroscopy is emerging as a method of choice to determine molecular distances in biomolecules in the angstrom to nanometer range. However, line broadening mechanisms in F ENDOR spectra can obscure the detected spin-dipolar coupling that encodes the distance information, thus limiting the resolution and accessible distance range. So far, the origin of these mechanisms has not been understood.
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