Encapsulation of biomacromolecules by soaking and co-crystallization into porous protein crystals of hemocyanin.
Biochem Biophys Res Commun
; 509(2): 577-584, 2019 02 05.
Article
em En
| MEDLINE
| ID: mdl-30600183
ABSTRACT
Encapsulation of guest molecules into the hollow spaces of crystals has been applied for a variety of purposes such as structure determination, separation, and catalysis of the guest. Although host-guest studies have been developed mainly in crystals of small molecules, those of biomacromolecules have recently been applied. In those reports, a huge hollow space in the protein crystal is commonly used for encapsulation of the guest. Our previous study revealed that cylindrical hemocyanins stack inside the crystal as a linear hollow structure. The diameter of the linear hollow is approximately 110â¯Å, which is large enough for most proteins to pass through. In the present study, we evaluated the potential of hemocyanin crystals as a host to encapsulate biomacromolecules. Confocal microscopy revealed that hemocyanin crystals encapsulate proteins of molecular mass up to 250â¯kDa, i.e., 27â¯kDa green fluorescence protein, 105â¯kDa allophycocyanin, 220â¯kDa C-phycocyanin, and 250â¯kDa phycoerythrin, and DNAs up to 200-bp long, whereas 440â¯kDa ferritin not. Further analysis revealed that hemocyanin crystals prefer a negatively charged guest rather than a positive charge to encapsulate. Moreover, a photobleaching experiment showed that the guest does not move once entrapped. This knowledge of the host-guest study using the hollow hemocyanin crystal should be of significance for further application of hollow proteinaceous crystals as a host.
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Base de dados:
MEDLINE
Assunto principal:
Decapodiformes
/
Hemocianinas
/
Cristalização
Limite:
Animals
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article