U.R. 1268 Biopolymères Interactions Assemblages (BIA), INRA, Rue de la Géraudière, 44316 Nantes, France.
Phys Chem Chem Phys. 2013 Jul 21;15(27):11339-48. doi: 10.1039/c3cp51007g. Epub 2013 Jun 4.
The present work was focused on the nanomechanical and adhesion properties of the napin (2S albumin) and cruciferin (12S globulin) rapeseed (Brassica napus L.) proteins, respectively, a low and high molecular weight seed protein. Using chemically modified AFM tips, force spectroscopy experiments demonstrated notable differences in the tip-protein interaction strength with regard to the nature of the protein and pH of the aqueous environment. The results clearly underline the role of residence time and electrostatic interactions in the protein-protein adhesion force. Although the nanomechanical experiments concerned more than a single molecule, unfolding length and force characteristics of the rapeseed proteins have been statistically found to be sensitive to the structural properties of the protein. This study provides insight into the characterization of rapeseed proteins and then a better knowledge of their interaction and assembling at the nanoscale range.
本工作主要研究了油菜籽（ Brassica napus L.）中低分子量的 napin（2S 白蛋白）和高分子量的 cruciferin（12S 球蛋白）的纳米力学和粘附特性。使用化学修饰的 AFM 针尖，力谱实验表明，针尖与蛋白质的相互作用强度取决于蛋白质的性质和水相环境的 pH 值。结果清楚地表明了停留时间和静电相互作用在蛋白质-蛋白质粘附力中的作用。尽管纳米力学实验涉及多个分子，但油菜籽蛋白的展开长度和力特性在统计学上被发现对蛋白质的结构特性敏感。本研究深入了解了油菜籽蛋白的特性，然后更好地了解了它们在纳米范围内的相互作用和组装。
