Templated Crystallization of Glycine Homopeptides: Experimental and Computational Developments
Templated Crystallization of Glycine Homopeptides: Experimental and Computational Developments
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甘氨酸同肽的模板化结晶：实验和计算进展
DOI：
10.1002/ceat.202200575
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发表时间：
2023
影响因子：
2.1
通讯作者：
Verma V
中科院分区：
文献类型：
--
作者：
Verma V
玻璃珠的使用作为非均相添加剂的结晶的甘氨酸homopeptides的研究，从而玻璃珠的实验显示，以增加结晶速率。诱导时间分析表明玻璃微珠的存在增强了成核动力学因子。这些结果进行了比较，由作者先前获得的甘氨酸和双甘氨酸，它表明，成核速率的增加是成正比的肽链长度。分子动力学模拟证实，较大的分子表现出更快的成核在玻璃珠的存在下，由于观察到的最长的氢键寿命为三甘氨酸，其次是二甘氨酸和甘氨酸的相互作用的数量增加。
The usage of glass beads as heterogeneous additives for the crystallization of glycine homopeptides is investigated, whereby glass beads are shown experimentally to increase the rate of crystallization. Induction time analysis indicates that the presence of glass beads acts enhances the kinetic factor for nucleation. These results are compared to those previously obtained by the authors for glycine and diglycine, and it is demonstrated that the increase in nucleation rate is proportional to the peptide chain length. Molecular dynamics simulations confirm that larger molecules exhibit faster nucleation in the presence of glass beads due to an increased number of interactions as observed with the longest hydrogen bond lifetime for triglycine, followed by diglycine and glycine.