Changes in the secondary structures and zeta potential of soybean peptide and its calcium complexes in different solution environments
Changes in the secondary structures and zeta potential of soybean peptide and its calcium complexes in different solution environments
复制标题
大豆肽及其钙配合物在不同溶液环境中二级结构和zeta电位的变化
DOI：
10.1039/d0fo03478a
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发表时间：
2021-04-07
期刊：
影响因子：
6.1
通讯作者：
Shuntang, Guo
中科院分区：
文献类型：
--
作者：
He, Liu;Ying, Lv;Shuntang, Guo
为了阐明大豆多肽及其钙络合物被跨膜吸附时环境疏水性的关系，采用不同的溶液环境(HBS缓冲液、TFE疏水溶液和细胞悬浮液)模拟了亲水和疏水环境。本研究采用酶解和超滤相结合的方法，制备了具有较高钙结合能力的大豆多肽(10-30 kDa)。细胞实验结果表明，该多肽能将钙转运到细胞内进行吸收。不同溶液环境下多肽及其钙络合物的二级结构变化表明，在跨膜吸收过程中，多肽的二级结构发生了变化，α-螺旋和β-折叠结构的含量增加。此外，多肽-钙复合体中的β-折叠结构进一步转化为α-螺旋结构。这种转化可能是由多肽溶液的疏水性引起的。此外，当构象发生变化时，样品中带正电荷的多肽会暴露出来，并与细胞相互作用，这有利于多肽-钙复合体的跨膜。
To illustrate the relationship between environment hydrophobicity and soybean peptide and its calcium complexes when they are absorbed transmembrane, different solution environments (HBS buffer, TFE hydrophobic solution and cell suspension) were used to simulate hydrophilic and hydrophobic environments. In this study, soybean peptides (10-30 kDa) with a high calcium binding capacity were prepared by enzymatic hydrolysis and ultrafiltration. The results of cell experiments showed that the peptide could transport calcium into cells for absorption. Secondary structure changes of the peptide and its calcium complexes in different solution environments showed that the secondary structure of the peptide changed during the transmembrane absorption, and the contents of alpha-helix and beta-sheet structures increased. Besides, the beta-sheet structures in the peptide-calcium complexes were further converted to an alpha-helix structure. This conversion may be induced by the hydrophobicity of peptide solutions. In addition, when the conformation changes, the positively charged peptides in the sample will be exposed and then interact with cells, which is beneficial for the transmembrane of peptide-calcium complexes.