Electron spin-echo envelope modulation (ESEEM) spectroscopy was used to investigate intramolecular and intermolecular complexes of cyclodextrins (CDs) with a nitroxide group. The interaction with solvent molecules (D(2)O) was followed through the (2)H modulation depth. Competition experiments with adamantane-type guests were used to confirm complexation. The shielding of the nitroxide group from solvent upon inclusion into a CD cavity made this technique more sensitive to complexation than cw EPR spectroscopy. ESEEM analysis of a series of CDs mono and bis spin-labeled on the primary rim of the cavity showed that only one compound formed a self-inclusion complex. This suggests that significant linker length/flexibility is required for formation of inclusion complexes in functionalized CDs. DEER (double electron-electron resonance) experiments confirmed that the self-inclusion complex of the spin-labeled CD was intra- rather than intermolecular.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1021/jp8099048 | DOI Listing |
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 PDFMol 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 PDFProc Natl Acad Sci U S A
December 2024
Department of Chemistry, Northwestern University, Evanston, IL 60208.
Mn coordinated by orthophosphate (Pi), metabolites, or peptides acts as a superoxide dismutase (SOD), and these Mn antioxidant complexes are universally accumulated in extremely radiation-resistant cell types across the tree of life. This behavior prompted design of decapeptide DP1 (DEHGTAVMLK) as a Mn ligand, and development of a highly potent Mn-antioxidant (MDP) containing [Pi] = 25 mM, and [DP1] = 3 mM, the ratio found in the radioresistant bacterium , with [Mn] = 1 mM. MDP is an exceptional antioxidant, both in vitro and in vivo, and has reinvigorated the development of radiation-inactivated whole-cell vaccines.
View Article and Find Full Text PDFLytic Polysaccharide Monooxygenases (LPMOs) catalyze the oxidative depolymerization of polysaccharides at a monocopper active site, that is coordinated by the so-called histidine brace. In the past, this motif has sparked considerable interest, mostly due to its ability to generate and stabilize highly oxidizing intermediates during catalysis. We used a variety of advanced EPR techniques, including Electron Nuclear Double Resonance (ENDOR), Electron Spin Echo Envelope Modulation (ESEEM) and Hyperfine Sublevel Correlation (HYSCORE) spectroscopy in combination with isotopic labelling (N, H) to characterize the active site of the bacterial LPMO AA10A over a wide pH range (pH 4.
View Article and Find Full Text PDFBiochim Biophys Acta Bioenerg
January 2025
Protein Crystallography, Faculty of Biology and Biotechnology, Ruhr University Bochum, 44801 Bochum, Germany. Electronic address:
Light harvesting proteins are optimized to efficiently collect and transfer light energy for photosynthesis. In eukaryotic dinoflagellates these complexes utilize chlorophylls and a special carotenoid, peridinin, and arrange them for efficient excitation energy transfer. At the same time, the carotenoids protect the system by quenching harmful chlorophyll triplet states.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!