Department of Bioresource Engineering, Faculty of Agricultural and Environmental Sciences , McGill University , Sainte-Anne-de-Bellevue , Québec H9X 3V9 , Canada.
Department of Biological Engineering, School of Engineering , University of Guelph , Guelph , Ontario N1G 2W1 , Canada.
J Agric Food Chem. 2019 Nov 13;67(45):12547-12557. doi: 10.1021/acs.jafc.9b05140. Epub 2019 Oct 29.
This study aims at understanding the changes in the structural properties of Gly m 4 soy allergen as a result of the influence of the temperature and pressure deviations. The primary emphasis was placed on analyzing the surface properties of suspected linear and conformational epitopes present in the Gly m 4 allergen. All three epitopes of Gly m 4 were studied, and the results showed that the molecule has significant structural changes in terms of solvent-accessible surface area (SASA) and radius of gyration, which showed that the increased pressures resulted in compaction. However, at lower temperatures and higher pressures (300 K and 6 kbar), swelling in the molecule was observed with a significant increase in the surface area. The study also tracked the changes in surface areas of individual residues that are part of the selected epitopes. Residues, such as D-27 and T-51, were found to have significant changes in their SASA as a result of temperature and pressure deviations.
本研究旨在探讨温度和压力偏差对 Gly m 4 大豆过敏原结构特性变化的影响。本研究重点分析了 Gly m 4 过敏原中疑似线性和构象表位的表面特性。对 Gly m 4 的三个表位进行了研究，结果表明，该分子在溶剂可及表面积（SASA）和回转半径方面发生了显著的结构变化，这表明增加的压力导致了分子的压缩。然而，在较低的温度和较高的压力（300 K 和 6 kbar）下，观察到分子的肿胀，表面积显著增加。该研究还跟踪了选定表位中个别残基的表面积变化。结果发现，D-27 和 T-51 等残基的 SASA 由于温度和压力偏差而发生了显著变化。
