Covalent modification is an effective strategy for reducing allergenicity to individual allergens, but there are few studies on this strategy modifying specific amino acids within epitopes under the influence of food matrix. This study used fucoidan to covalently modify shrimp () and combined mass spectrometry and bioinformatics techniques to explore epitope modification. The results showed that lower concentrations (<2.50%) of fucoidan facilitated the covalent modification reaction and effectively modified amino acid sites in the loop regions of allergens, including lysine, asparagine, and methionine. In contrast, higher concentrations (>5.00%) of fucoidan hindered the reaction and modified amino acid sites in the helix regions of allergens, including asparagine, lysine, and methionine. The RBL-2H3 cells model confirmed that modification of hemocyanin epitopes was the main reason for reduced allergenicity. Overall, fucoidan-mediated covalent modification can effectively modify various allergenic epitopes in shrimp, which is a potential strategy to reduce shrimp allergenicity.
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http://dx.doi.org/10.1021/acs.jafc.5c01115 | DOI Listing |
J Agric Food Chem
March 2025
SKL of Marine Food Processing & Safety Control, National Engineering Research Center of Seafood, School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China.
Covalent modification is an effective strategy for reducing allergenicity to individual allergens, but there are few studies on this strategy modifying specific amino acids within epitopes under the influence of food matrix. This study used fucoidan to covalently modify shrimp () and combined mass spectrometry and bioinformatics techniques to explore epitope modification. The results showed that lower concentrations (<2.
View Article and Find Full Text PDFFood Funct
March 2025
College of Food Science and Engineering, Nanjing University of Finance and Economics/Collaborative Innovation Center for Modern Grain Circulation and Safety, Nanjing 210023, China.
Lactoferrin (LF) and epigallocatechin gallate (EGCG) are recognized for their potent osteogenic properties. However, the osteogenic activity of LF-EGCG complexes is not fully understood. In this study, both non-covalent and covalent LF-EGCG complexes with different LF : EGCG ratios were prepared, and their effects on the LF structure and thermal stability were investigated using circular dichroism, Fourier transform infrared spectroscopy, fluorescence spectroscopy, Raman spectroscopy, and differential scanning calorimetry.
View Article and Find Full Text PDFChem Rec
March 2025
College of Chemistry & Chemical Engineering, Qingdao University, Qingdao, 266071, China.
Biomolecule-engineered metal-organic frameworks (Bio-MOFs) are designed by incorporating biomolecules into or onto MOFs through covalent and non-covalent interactions. These composite frameworks exhibit unique catalytic and biological activities, making them highly suitable for various biocatalytic applications. In this review, we highlight recent advances in the material design, bioengineering methods, structural and functional regulation techniques, and biocatalytic applications of Bio-MOFs.
View Article and Find Full Text PDFChemistry
March 2025
Shanghai Institute of Materia Medica Chinese Academy of Sciences, Department of Molecular Pharmacology, 555 Zuchiongzhi Road, 201203, Shanghai, CHINA.
Sortase A (SrtA), a cysteine transpeptidase critical for surface protein anchoring in Gram-positive pathogens, represents an attractive antivirulence target. While covalent SrtA inhibitors show therapeutic potential, existing compounds lack species selectivity. Through structure-guided design, we developed T10, a covalent inhibitor selectively targeting Streptococcus pyogenes SrtA (SpSrtA) over Staphylococcus aureus SrtA (SaSrtA).
View Article and Find Full Text PDFDev Cell
March 2025
Max Perutz Labs, Department of Biochemistry and Cell Biology, University of Vienna, A1030 Vienna, Austria. Electronic address:
SUMOylation is a reversible post-translational modification that contributes to various biological processes in plants. In this issue of Developmental Cell, Zhang et al. show that covalent attachment of SUMO to PROPEP proteins promotes their proteolytic cleavage by metacaspase to release small signaling peptides (plant elictor peptides [PEPs]), triggering the release of the mature peptide in response to cell wall damage.
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