热稳定性
盐桥
聚对苯二甲酸乙二醇酯
热稳定性
降级(电信)
分子动力学
材料科学
残留物(化学)
盐(化学)
化学
化学工程
生物系统
计算机科学
酶
复合材料
计算化学
有机化学
生物
突变体
生物化学
工程类
电信
基因
作者
Qu Zhi,Kun Chen,Lin Zhang,Yan Sun
出处
期刊:ChemBioChem
[Wiley]
日期:2023-09-13
卷期号:24 (21)
被引量:3
标识
DOI:10.1002/cbic.202300373
摘要
Polyethylene terephthalate (PET) is one of the most widely used plastics, and the accumulation of PET poses a great threat to the environment. IsPETase can degrade PET rapidly at moderate temperatures, but its application is greatly limited by the low stability. Herein, molecular dynamics (MD) simulations combined with a sequence alignment strategy were adopted to introduce salt bridges into the flexible region of IsPETase to improve its thermal stability. In the designed variants, the Tm values of IsPETaseI168R/S188D and IsPETaseI168R/S188E were 7.4 and 8.7 °C higher than that of the wild type, respectively. The release of products degraded by IsPETaseI168R/S188E was 4.3 times that of the wild type. Tertiary structure characterization demonstrated that the structure of the variants IsPETaseI168R/S188D and IsPETaseI168R/S188E became more compact. Extensive MD simulations verified that a stable salt bridge was formed between the residue R168 and D186 in IsPETaseI168R/S188D , while in IsPETaseI168R/S188E an R168-D186-E188 salt bridge network was observed. These results confirmed that the proposed computation-based salt bridge design strategy could efficiently generate variants with enhanced thermal stability for the long-term degradation of PET, which would be helpful for the design of enzymes with improved stability.
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