Gao Jingjing, Wang Hui, Zhuang Jiaming, Thayumanavan S
Department of Chemistry , University of Massachusetts Amherst , Amherst , MA 01003 , USA . Email:
U.S. Army Edgewood Chemical Biological Center , 8198 Blackhawk Road, Aberdeen Proving Ground , MD 21010 , USA.
Chem Sci. 2019 Jan 15;10(10):3018-3024. doi: 10.1039/c8sc04744h. eCollection 2019 Mar 14.
Developing design rules that offer tailorability in materials' response to enzymes is of great importance, as such materials are of interest in a variety of biomedical applications including sensing, diagnostics and drug delivery. Using an amphiphilic oligomeric platform, we show that the degree of polymerization and hydrophilic-lipophilic balance variations can be utilized to alter the unimer-aggregate equilibrium, which in turn offers robust tunability of the host-guest properties of the amphiphilic nanoassemblies. We found that oligomeric assemblies with higher degree of polymerization are less sensitive to enzymatic degradation and release the guest molecules at a slower rate. Similarly, increasing the hydrophilicity makes these assemblies more sensitive to enzymes. These trends can be understood by correlating these changes to predictable modifications in the dynamics of the unimer-aggregate equilibrium, which affects the substrate availability for enzymes. These findings provide insights into rationally tuning the response of enzyme-sensitive supramolecular assemblies.
制定能够使材料对酶的反应具有可定制性的设计规则非常重要，因为这类材料在包括传感、诊断和药物递送在内的各种生物医学应用中都备受关注。利用两亲性低聚物平台，我们表明聚合度和亲水-亲脂平衡的变化可用于改变单体-聚集体平衡，这反过来又为两亲性纳米组装体的主客体性质提供了强大的可调性。我们发现，聚合度较高的低聚物组装体对酶促降解的敏感性较低，释放客体分子的速度较慢。同样，增加亲水性会使这些组装体对酶更敏感。通过将这些变化与单体-聚集体平衡动力学中可预测的修饰相关联，可以理解这些趋势，而单体-聚集体平衡动力学的变化会影响酶的底物可用性。这些发现为合理调节酶敏感超分子组装体的反应提供了见解。
