Nanomechanics of Pectin-Linked ß-Lactoglobulin Nanofibril Bundles.
Nanomechanics of Pectin-Linked ß-Lactoglobulin Nanofibril Bundles.
复制标题
果胶连接的乳球蛋白纳米纤维束的纳米力学。
DOI：
10.1021/acs.biomac.8b00408
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发表时间：
2018
影响因子：
6.2
通讯作者：
Loveday SM
中科院分区：
文献类型：
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作者：
Loveday SM
β-乳球蛋白的纳米原纤维可以通过与高甲氧基果胶的位点特异性非共价交联组装成束（Hettiarachchi等人，Soft Matter 2016，12，756）。在这里，我们使用原子力显微镜和力谱的特点束的纳米力学性能。束具有高斯截面，平均高度为17.4 ± 1.4 nm。使用均方端到端模型的图像分析计算持久性长度。持续长度和厚度之间的关系具有1.69-2.30的指数，这与以前报道的其他纤维类型一致。在力谱实验中，纤维束以与原纤维性质不同的方式拉伸，并且一些力曲线与从纤维束剥离原纤维一致。果胶连接的纳米原纤维束的柔性可能是可调的，通过调节原纤维的刚度和长度以及果胶与原纤维的比率，产生广泛的结构和功能。
Nanofibrils of β-lactoglobulin can be assembled into bundles by site-specific noncovalent cross-linking with high-methoxyl pectin (Hettiarachchi et al.Soft Matter2016,12, 756). Here we characterized the nanomechanical properties of bundles using atomic force microscopy and force spectroscopy. Bundles had Gaussian cross sections and a mean height of 17.4 ± 1.4 nm. Persistence lengths were calculated using image analysis with the mean-squared end-to-end model. The relationship between the persistence length and the thickness had exponents of 1.69–2.30, which is consistent with previous reports for other fibril types. In force spectroscopy experiments, the bundles stretched in a qualitatively different manner to fibrils, and some of the force curves were consistent with peeling fibrils away from bundles. The flexibility of pectin-linked nanofibril bundles is likely to be tunable by modulating the stiffness and length of fibrils and the ratio of pectin to fibrils, giving rise to a wide range of structures and functionalities.