| Literature DB >> 30372977 |
Liangtao Lv1, Hong Lin1, Zhenxing Li2, Balunkeswar Nayak3, Ishfaq Ahmed1, Shenglan Tian1, Guanzhi Chen4, Hang Lin4, Jinxia Zhao4.
Abstract
The aim of this study was to analyze the effect of AAPH on the conformational structure and allergenicity of shrimp tropomyosin (TM). The structure of AAPH-TM was evaluated by SDS-PAGE, fluorescence, circular dichroism (CD) and ultraviolet light (UV), and the allergenicity was evaluated by in vivo and in vitro methods. Results showed that AAPH can induce structural changes through TM aggregations. These aggregations can decrease the IgG/IgE binding capacity on immunoblot analysis. Further competitive inhibition ELISA (ciELISA) results showed the IC50 of AAPH-TM (AAPH 0-25 mmol/l) changed from 0.086 to 46.2 μg/ml, which correlated with TM structural changes. An RBL-2H3 cell assay showed that release rate of β-hexosaminidase and histamine decreased by 51.6% and 68.1% with AAPH (5 mmol/l) treatment, respectively. A mouse model showed AAPH-TM could decrease levels of IgE/IgG1, release of histamine and mMCP-1 in sera. In conclusion, AAPH induced TM aggregation can cause structural changes and decrease the allergenicity.Entities:
Keywords: 1-Anilino-8-naphthalene-sulfonate (PubChem CID: 1369); 3,3′,5,5′-Tetramethylbenzidine (PubChem CID: 41206); AAPH; Acrylamide (PubChem CID: 6579); Allergenicity; Brilliant Blue R (PubChem CID: 61365); DL-Dithiothreitol (PubChem CID: 446094); DL-lysine (PubChem CID: 866); L-leucine (PubChem CID: 6106); Protein oxidation; Shrimp tropomyosin
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Year: 2018 PMID: 30372977 DOI: 10.1016/j.foodchem.2018.09.030
Source DB: PubMed Journal: Food Chem ISSN: 0308-8146 Impact factor: 7.514