Acrolein (ACR) is an α,β-unsaturated aldehyde with high reactivity towards nucleophiles in proteins. In this study, a typical phenolic compound phloretin (Phl) was employed to counteract protein modification induced by ACR (1 mM) in whey protein isolate (WPI, 10 mg/mL). The addition of Phl (2 mM) significantly reduced ACR-induced surge of protein carbonyls (from 1.65 to 0.65 μmol/mg protein) and loss of protein total sulfhydryl content (from 0.28 to 0.24 μmol/mg protein) whilst contributing to further reductions in protein surface hydrophobicity and intrinsic fluorescence. The incorporation of ACR into WPI was effectively interrupted by Phl as visualized by Western blot. Only 2.87 % of ACR remained in the presence of 2 mM Phl with the generation of Phl-ACR adducts, suggesting Phl could partially alleviate protein modification by scavenging of ACR. These findings could have important implications for employment of natural phenolic nucleophiles against the adverse effects of ACR towards dietary proteins.
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http://dx.doi.org/10.1016/j.fochx.2024.102027 | DOI Listing |
Photosynth Res
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Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia.
The Orange Carotenoid Protein (OCP) is a unique water-soluble photoactive protein that plays a critical role in regulating the balance between light harvesting and photoprotective responses in cyanobacteria. The challenge in understanding OCP´s photoactivation mechanism stems from the heterogeneity of the initial configurations of its embedded ketocarotenoid, which in the dark-adapted state can form up to two hydrogen bonds to critical amino acids in the protein's C-terminal domain, and the extremely low quantum yield of primary photoproduct formation. While a series of experiments involving point mutations within these contacts helped us to identify these challenges, they did not resolve them.
View Article and Find Full Text PDFChem Asian J
January 2025
Indian Institute of Science, Inorganic and Physical Chemistry, Indian Institute of Science, 560 012, Bangalore, INDIA.
Intracellular delivery of proteins is an important barrier in the development of strategies to deliver functional proteins and protein therapeutics into the cells to realize their full potential in biotechnology, biomedicine, cell-based therapies, and gene editing protein systems. Most of the intracellular protein delivery strategies involve the conjugation of cell penetrating peptides to enable and enhance the permeability of plasma membrane of mammalian cells to allow proteins to enter cytosol. Small molecules conjugations such as (p-methylphenyl) glycine, pyrenebutyrate and cysteines are used for the same purpose.
View Article and Find Full Text PDFFASEB J
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Department of Nephropathy, The First Affiliated Hospital of Anhui Medical University, Anhui Medical University, Hefei, Anhui, People's Republic of China.
Macrophage infiltration and activation is a key factor in the progression of diabetic nephropathy (DN). However, aerobic glycolysis induced by m6A methylation modification plays a key role in M1-type activation of macrophages, but the specific mechanism remains unclear in DN. In this study, the expression of m6A demethylase Fto in bone marrow derived macrophages and primary kidney macrophages from db/db mice.
View Article and Find Full Text PDFOrg Biomol Chem
January 2025
Department of Chemistry, Muragachha Government College, Nadia 741154, West Bengal, India.
In spite of being the second-lowest abundant proteinogenic amino acid, approximately 90% of proteins contain at least one tryptophan residue. Hence, the chemoselective functionalization of tryptophan residue can provide access to site-selective bioconjugation of almost all known proteins. With the increase in the utility of bioconjugated proteins and peptides as drugs and therapeutic agents, the development of smart protocols to fabricate and modulate biomolecules has flourished.
View Article and Find Full Text PDFNucleic Acids Res
January 2025
Department of Health Sciences and Technology, ETH Zurich, Schmelzbergstrasse 9, Zurich 8092, Switzerland.
Temozolomide kills cancer cells by forming O6-methylguanine (O6-MeG), which leads to cell cycle arrest and apoptosis. However, O6-MeG repair by O6-methylguanine-DNA methyltransferase (MGMT) contributes to drug resistance. Characterizing genomic profiles of O6-MeG could elucidate how O6-MeG accumulation is influenced by repair, but there are no methods to map genomic locations of O6-MeG.
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