利用 H NMR 自旋晶格（）弛豫时间研究 α-角蛋白中的分子相互作用和分配。
Molecular interaction and partitioning in α-keratin using H NMR spin-lattice () relaxation times.
机构信息
Institute of Chemical Biology, Department of Chemistry, MSRH, Imperial College London, White City Campus, 80-92 Wood Lane, London W12 0BZ, UK.
Department of Chemical Engineering, Imperial College London, South Kensington Campus, London SW7 2AZ, UK.
出版信息
J R Soc Interface. 2021 Dec;18(185):20210698. doi: 10.1098/rsif.2021.0698. Epub 2021 Dec 8.
The interactions between small molecules and keratins are poorly understood. In this paper, a nuclear magnetic resonance method is presented to measure changes in the H relaxation times of small molecules in human hair keratin to quantify their interaction with the fibre. Two populations of small-molecule compounds were identified with distinct relaxation times, demonstrating the partitioning of the compounds into different keratin environments. The changes in relaxation time for solvent in hair compared with bulk solvent were shown to be related to the molecular weight (MW) and the partition coefficient, LogP, of the solvent investigated. Compounds with low MWs and high hydrophilicities had greater reductions in their relaxation times and therefore experienced increased interactions with the hair fibre. The relative population sizes were also calculated. This is a significant step towards modelling the behaviour of small molecules in keratinous materials and other large insoluble fibrous proteins.
小分子与角蛋白的相互作用还不太清楚。本文提出了一种核磁共振方法，用于测量小分子在人发角蛋白中的 H 弛豫时间的变化，以定量它们与纤维的相互作用。确定了两种具有不同弛豫时间的小分子化合物群体，证明了化合物在不同角蛋白环境中的分配。与体相溶剂相比，头发中溶剂的弛豫时间变化与溶剂的分子量 (MW) 和分配系数 LogP 有关。MW 低且亲水性高的化合物的弛豫时间降低幅度更大，因此与头发纤维的相互作用增加。还计算了相对种群大小。这是朝着模拟小分子在角蛋白材料和其他不溶性纤维状蛋白质中的行为迈出的重要一步。
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