Self-assembly in the transparent droplets formed during the screening of protein self-assembly conditions.
- Author:
Tuodi ZHANG
1
;
Xudong DENG
1
;
Fengzhu ZHAO
1
;
Wenpu SHI
1
;
Liangliang CHEN
1
;
Yaqing ZHOU
1
;
Xueting WANG
1
;
Chenyan ZHANG
1
;
Dachuan YIN
1
Author Information
- Publication Type:Journal Article
- Keywords: Index™ C10; clear droplets; micro- and nano-scale protein assembly; β-lactoglobulin
- MeSH: Crystallization; Lactoglobulins
- From: Chinese Journal of Biotechnology 2021;37(4):1396-1405
- CountryChina
- Language:Chinese
- Abstract: Protein self-assemblies at the micro- and nano-scale are of great interest because of their morphological diversity and good biocompatibility. High-throughput screening of protein self-assembly at different scales and morphologies using protein crystallization screening conditions is an emerging method. When using this method to screen protein self-assembly conditions, some apparently transparent droplets are often observed, in which it is not clear whether self-assembly occurs. We explored the interaction between β-lactoglobulin and the protein crystallization kit Index™ C10 and observed the presence of micro- and nano-scale protein self-assemblies in the transparent droplets. The diverse morphology of the micro- and nano-scale self-assemblies in the transparent droplets formed by mixing different initial concentrations of β-lactoglobulin and Index™ C10 was further investigated by scanning electron microscope. Self-assembly process of fluorescence-labelled β-lactoglobulin was monitored continuously by laser confocal microscope, allowing real-time observation of the liquid-liquid phase separation phenomenon and the morphology of the final self-assemblies. The internal structure of the self-assemblies was gradually ordered over time by in-situ X-ray diffraction. This indicates that the self-assembly phenomenon within transparent droplets, observed in protein self-assembly condition screening experiments, is worthy of further in-depth exploration.
