The adsorbed conformation of globular proteins at the air/water interface
The adsorbed conformation of globular proteins at the air/water interface
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DOI：
10.1039/b515934b
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发表时间：
2006-05-14
影响因子：
3.3
通讯作者：
Green, Rebecca J.
中科院分区：
文献类型：
--
作者：
Lad, Mitaben D.;Birembaut, Fabrice;Green, Rebecca J.
外反射FTIR光谱和表面压力测量被用来比较在空气/水界面的吸附结构的三个球状蛋白质的构象变化。在所研究的三种蛋白质（溶菌酶、牛血清白蛋白和P-乳球蛋白）中，溶菌酶的行为是独特的。溶菌酶吸附缓慢，需要约2.5小时才能达到表面压力平台（从0.07 mM溶液），并导致显着的结构变化。FTIR光谱显示，溶菌酶形成了一个高度网络化的未折叠蛋白质的吸附层，具有高反平行β-折叠含量，这些变化发生迅速（10分钟内）。这种非天然的二级结构类似于3D热定型蛋白质凝胶，表明吸附的蛋白质形成了高度网络化的界面层。白蛋白和β-乳球蛋白吸附迅速（在10分钟内达到平台期），几乎没有机会进入其天然二级结构。
External reflection FTIR spectroscopy and surface pressure measurements were used to compare conformational changes in the adsorbed structures of three globular proteins at the air/water interface. Of the three proteins studied, lysozyme, bovine serum albumin and P-lactoglobulin, lysozyme was unique in its behaviour. Lysozyme adsorption was slow, taking approximately 2.5 h to reach a surface pressure plateau (from a 0.07 mM solution), and led to significant structural change. The FTIR spectra revealed that lysozyme formed a highly networked adsorbed layer of unfolded protein with high antiparallel beta-sheet content and that these changes occurred rapidly (within 10 min). This non-native secondary structure is analogous to that of a 3D heat-set protein gel, suggesting that the adsorbed protein formed a highly networked interfacial layer. Albumin and P-lactoglobulin adsorbed rapidly (reaching a plateau within 10 min) and with little chance to their native secondary structure.