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Extraordinary SERS on nanostructured self-assembled silver films due to preliminary random nano-profiling of substrate and ultrasonic exposure of analyte during the deposition.
Spectrochim Acta A Mol Biomol Spectrosc
December 2024
Institute for Theoretical and Applied Electromagnetics RAS, Moscow 125412, Russia; Moscow Institute of Physics and Technology, Dolgoprudny, Moscow Region 141700, Russia.
In this study, we have investigated the surface-enhanced Raman scattering (SERS) spectra of myoglobin on silver substrates with different morphology. The aim was to determine the optimal parameters of analyte and substrate preparation for obtaining of high-amplitude SERS spectra of proteins. It is shown that not only the morphology of the silver film, but also the method of analyte molecules deposition on the SERS substrate plays an important role.
View Article and Find Full Text PDFExploring Compactness and Dynamics of Apomyoglobin.
Proteins
December 2024
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Russia.
Hydrogen-deuterium exchange mass spectrometry (HDX-MS) approach has become a valuable analytical complement to traditional methods. HDX-MS allows the identification of dynamic surfaces in proteins. We have shown that the introduction of various mutations into the amino acid sequence of whale apomyoglobin (apoMb) leads to a change in the number of exchangeable hydrogen atoms, which is associated with a change in its compactness in the native-like condition.
View Article and Find Full Text PDFOptimization Function for Determining Optimal Dose Range for Beef and Seed Potato Irradiation.
Foods
November 2024
Department of Chemistry, Lomonosov Moscow State University, GSP-1, 1-3 Leninskiye Gory, 119991 Moscow, Russia.
The objective of this study is to develop a universally applicable approach for establishing the optimal dose range for the irradiation of plant and animal products. The approach involves the use of the optimization function for establishing the optimal irradiation dose range for each category of plant and animal product to maximize the suppression of targeted pathogens while preserving the surrounding molecules and biological structures. The proposed function implies that pathogens found in the product can be efficiently suppressed provided that irradiation is performed with the following criteria in mind: a high irradiation dose uniformity, a high probability of irradiation hitting pathogens and controlled heterogeneity of radiobiological sensitivity of pathogens.
View Article and Find Full Text PDFConstruction of a Convenient and Highly Sensitive Sensor for the Detection of Myo in Serum Based on ELI-SERS.
ACS Sens
December 2024
College of Optical and Electronic Technology, China Jiliang University, Hangzhou 310018, China.
Acute myocardial infarction (AMI) is one of the most common causes of sudden death in cardiovascular disease, and myoglobin (Myo) is the first protein to be released in the blood after the attack, which is an important biomarker for clinical detection of AMI. The "Golden Rescue Time" for acute myocardial infarction is to intervene within the first 30 min after the attack; therefore, a rapid and accurate Myo detection method is needed urgently. In this study, we designed a combined enzyme-linked immunosorbent assay (ELISA) technique with surface-enhanced Raman scattering (SERS) immunoassay (ELI-SERS), which integrates the small sample volume, ease of operation, and excellent linearity of ELISA while utilizing the SERS technique and selecting the molecule with the Raman signal (IR-808), which is in resonance with the excitation wavelength, for further signal enhancement.
View Article and Find Full Text PDFImpact of yohimbine on myoglobin stability: insights from molecular spectroscopic, and computational approaches.
J Biomol Struct Dyn
November 2024
Department of Chemistry, National Institute of Technology Nagaland, Dimapur, Nagaland, India.
Article Synopsis
- The study focuses on the interaction between the bioactive ligand yohimbine (Yoh) and the protein myoglobin (Mb), highlighting its importance in pharmacokinetics and pharmacodynamics.
- Through emission spectroscopy, it was found that Yoh has a binding constant of 10 M and a 1:1 binding site ratio with Mb, while structural changes in Mb were observed using circular dichroism.
- The validation of binding interactions was supported by molecular dynamics simulations, showing that the Mb-Yoh complex remains stable over time, which is crucial for understanding drug design and bioavailability.
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