Spatiotemporal control of l-phenylalanine crystallization in microemulsion: the role of water in mediating molecular self-assembly
Qi Liu,
Jingkang Wang,
Xin Huang,
Hao Wu,
Shuyi Zong,
Xiaowei Cheng,
Hongxun Hao
Affiliations
Qi Liu
National Engineering Research Center of Industrial Crystallization Technology, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, People's Republic of China
Jingkang Wang
National Engineering Research Center of Industrial Crystallization Technology, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, People's Republic of China
Xin Huang
National Engineering Research Center of Industrial Crystallization Technology, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, People's Republic of China
Hao Wu
National Engineering Research Center of Industrial Crystallization Technology, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, People's Republic of China
Shuyi Zong
National Engineering Research Center of Industrial Crystallization Technology, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, People's Republic of China
Xiaowei Cheng
National Engineering Research Center of Industrial Crystallization Technology, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, People's Republic of China
Hongxun Hao
National Engineering Research Center of Industrial Crystallization Technology, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, People's Republic of China
Water confined or constrained in a cellular environment can exhibit a diverse structural and dynamical role and hence will affect the self-assembly behavior of biomolecules. Herein, the role of water in the formation of l-phenylalanine crystals and amyloid fibrils was investigated. A microemulsion biomimetic system with controllable water pool size was employed to provide a microenvironment with different types of water, which was characterized by small-angle X-ray scattering, attenuated total reflectance-Fourier transform infrared spectroscopy and differential scanning calorimetry. In a bound water environment, only plate-like l-phenylalanine crystals and their aggregates were formed, all of which are anhydrous crystal form I. However, when free water dominated, amyloid fibrils were observed. Free water not only stabilizes new oligomers in the initial nucleation stage but also forms bridged hydrogen bonds to induce vertical stacking to form a fibrous structure. The conformational changes of l-phenylalanine in different environments were detected by NMR. Different types of water trigger different nucleation and growth pathways, providing a new perspective for understanding molecular self-assembly in nanoconfinement.
