AI Article Synopsis
- Polyoxometalates (POMs) are complex nanoclusters that can interact with biomolecules like proteins, but their binding mechanisms are not fully understood.
- A study investigated the interaction between a specific POM, K13[Eu(SiW9Mo2O39)2], and bovine serum albumin (BSA), revealing a unique two-step binding process.
- The findings enhance our understanding of how the charge of POMs influences their interactions with proteins, paving the way for potential applications in developing inorganic drugs.
Article Abstract
Polyoxometalates (POMs) represent a type of typical polyanionic nanoclusters that can be utilized as inorganic bioactive materials; however, the detailed interactions of them with many target biomolecules such as peptides and proteins were not well clarified due to the complexity of the binding process. In the present study, the binding-induced physiochemical phenomena of a highly charged Eu-containing polyoxometalate, K13[Eu(SiW9Mo2O39)2] (EuSiWMo), with a model protein, bovine serum albumin (BSA), was identified upon the examination of luminescence of both the components during the titration. The large emission enhancement and subsequent quenching of the EuSiWMo were found in close relation to the amount of added BSA. Being different from the known binding type of less charged POMs, a distinct two-step binding process was concluded, and the possible mechanism was proposed through the analysis on the time-resolved fluorescence spectra, isothermal titration calorimetry (ITC), transmission electron microscope (TEM), and two-dimensional correlation spectroscopy (2D COS). The present results directed a new understanding for the charge numbers and existing state of POMs affecting the interaction with proteins, which is important to exploit the biological functionalities of POMs in related systems and the development of POMs as potential inorganic drugs.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1021/acs.langmuir.5b02868 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Development of targeted antimicrobial peptides for Escherichia coli: Combining phage display and rational design for food safety application.
Food Chem
December 2024
Laboratory of Molecular Nutrition and Immunity, College of Animal Science and Technology, Northeast Agricultural University, Harbin, PR China. Electronic address:
The growing demand for minimally processed foods has heightened the risk of pathogenic contamination. Balancing antimicrobial efficacy with the preservation of probiotic activity remains a significant challenge. In this study, we employed phage display peptide library screening, combined with next-generation sequencing to identify the HIMPIQA domain, which selectively targets pathogenic Escherichia coli (E.
View Article and Find Full Text PDFComparison of new secondgeneration H1 receptor blockers with some molecules; a study involving DFT, molecular docking, ADMET, biological target and activity.
BMC Chem
January 2025
Energy Systems Engineering Department, Engineering Faculty, Adana Alparslan Türkeş Science and Technology University, 01250, Adana, Türkiye.
Although the antiallergic properties of compounds such as CAPE, Melatonin, Curcumin, and Vitamin C have been poorly discussed by experimental studies, the antiallergic properties of these famous molecules have never been discussed with calculations. The histamine-1 receptor (H1R) belongs to the family of rhodopsin-like G-protein-coupled receptors expressed in cells that mediate allergies and other pathophysiological diseases. In this study, pharmacological activities of FDA-approved second generation H1 antihistamines (Levocetirizine, desloratadine and fexofenadine) and molecules such as CAPE, Melatonin, Curcumin, Vitamin C, ADMET (Absorption, Distribution, Metabolism, Excretion, Toxicity) profiles, density functional theory (DFT), molecular docking, biological targets and activities were compared by calculating.
View Article and Find Full Text PDFMolecular basis of JAK kinase regulation guiding therapeutic approaches: Evaluating the JAK3 pseudokinase domain as a drug target.
Adv Biol Regul
December 2024
Faculty of Medicine and Health Technology, Tampere University, Arvo Ylpönkatu 34, 33014, Finland; Institute of Biotechnology, HiLIFE, University of Helsinki, P.O. Box 56, 00014, Finland; Department of Microbiology, Fimlab Laboratories, P.O.Box 66, 33013, Tampere, Finland. Electronic address:
Janus kinases (JAK1-3, TYK2) are critical mediators of cytokine signaling and their role in hematological and inflammatory and autoimmune diseases has sparked widespread interest in their therapeutic targeting. JAKs have unique tandem kinase structure consisting of an active tyrosine kinase domain adjacent to a pseudokinase domain that is a hotspot for pathogenic mutations. The development of JAK inhibitors has focused on the active kinase domain and the developed drugs have demonstrated good clinical efficacy but due to off-target inhibition cause also side-effects and carry a black box warning limiting their use.
View Article and Find Full Text PDFSubstrate-specific responses to mixing conditions in high-solids enzymatic hydrolysis: Insights from microcrystalline cellulose and dilute-acid pretreated corncob.
Int J Biol Macromol
January 2025
Jiangsu Co-Innovation Center of Efficient Processing and Utilization of Forest, Resources, College of Chemical Engineering, Nanjing Forestry University, Nanjing 210037, PR China. Electronic address:
This study investigates the mixing effects on the enzymatic hydrolysis of microcrystalline cellulose (MCC) and dilute-acid pretreated corncob substrates under high-solid conditions. Enzymatic hydrolysis experiments were conducted to assess cellulose conversion rates under varying mixing conditions (0, 50, 150, and 250 rpm) and solids loadings (5 %, 15 %, 25 %, and 35 %, w/v), and distinct physicochemical properties of the substrates were characterized. Additionally, the role of mixing conditions and solid loadings on cellulose hydrolysis kinetics and enzyme adsorption on both substrates and lignin were elucidated.
View Article and Find Full Text PDFThe RNA-binding properties of Annexins.
J Mol Biol
January 2025
Elettra Sincrotrone Trieste, Italy; The Wohl Institute, King's College London, 5 Cutcombe Rd, SW59RT London, UK. Electronic address:
Annexins are a family of calcium-dependent phospholipid-binding proteins involved in crucial cellular processes such as cell division, calcium signaling, vesicle trafficking, membrane repair, and apoptosis. In addition to these properties, Annexins have also been shown to bind RNA, although this function is not universally recognized. In the attempt to clarify this important issue, we employed an integrated combination of experimental and computational approaches.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!