Protein Repellency of Well-Defined, Concentrated Poly(2-hydroxyethyl methacrylate) Brushes by the Size-Exclusion Effect

2006 ◽  
Vol 39 (6) ◽  
pp. 2284-2290 ◽  
Author(s):  
Chiaki Yoshikawa ◽  
Atsushi Goto ◽  
Yoshinobu Tsujii ◽  
Takeshi Fukuda ◽  
Tsuyoshi Kimura ◽  
...  
2020 ◽  
Author(s):  
Nikola Lončar ◽  
Henriette J. Rozeboom ◽  
Linda E. Franken ◽  
Marc C. A. Stuart ◽  
Marco Fraaije

In this paper, we report on the discovery of a novel, robust protein cage (encapsulin) that we could use for packaging various biocatalysts. We have elucidated the structure of the stable encapsulin by electron microscopy and X-ray diffraction. Furthermore, we developed an effective expression system for the encapsulin and a facile protocol for preparing encapsulated enzymes. By packaging and testing various enzymes (varying in size, oligomeric structure, and cofactor type) we demonstrate that, through encapsulation, the enzymes become significantly more stable. We also provide evidence that the pores of the encapsulin, through a size-exclusion effect, can modulate the substrate acceptance profile of an encapsulated enzyme.


2018 ◽  
Vol 20 (41) ◽  
pp. 26105-26116 ◽  
Author(s):  
Askar K. Gatiatulin ◽  
Viktoria Yu. Osel'skaya ◽  
Marat A. Ziganshin ◽  
Valery V. Gorbatchuk

The size exclusion of guests by α-cyclodextrin (aCD) in binary host–guest systems was observed to be a key structure–property relationship for the choice of this host as a receptor.


2020 ◽  
Author(s):  
Nikola Lončar ◽  
Henriette J. Rozeboom ◽  
Linda E. Franken ◽  
Marc C. A. Stuart ◽  
Marco Fraaije

In this paper, we report on the discovery of a novel, robust protein cage (encapsulin) that we could use for packaging various biocatalysts. We have elucidated the structure of the stable encapsulin by electron microscopy and X-ray diffraction. Furthermore, we developed an effective expression system for the encapsulin and a facile protocol for preparing encapsulated enzymes. By packaging and testing various enzymes (varying in size, oligomeric structure, and cofactor type) we demonstrate that, through encapsulation, the enzymes become significantly more stable. We also provide evidence that the pores of the encapsulin, through a size-exclusion effect, can modulate the substrate acceptance profile of an encapsulated enzyme.


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