Journal
APPLIED NANOSCIENCE
Volume 6, Issue 7, Pages 951-957Publisher
SPRINGER HEIDELBERG
DOI: 10.1007/s13204-015-0511-x
Keywords
Zeolitic imidazolate framework (ZIF-8); Proteins; BSA; Successive adsorption
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Funding
- Director of CSIR-CSIO, Chandigarh, India
- CSIR, India [OMEGA/PSC0202]
- National Research Foundation of Korea (NRF) - Ministry of Education, Science, and Technology (MEST) [2009-0093848]
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The robustness of biomolecules is always a significant challenge in the application of biostorage in biotechnology or pharmaceutical research. To learn more about biostorage in porous materials, we investigated the feasibility of using zeolite imidazolate framework (ZIF-8) with respect to protein encapsulation. Here, bovine serum albumin (BSA) was selected as a model protein for encapsulation with the synthesis of ZIF-8 using water as a media. ZIF-8 exhibited excellent protein adsorption capacity through successive adsorption of free BSA with the formation of hollow crystals. The loading of protein in ZIF-8 crystals is affected by the molecular weight due to diffusion-limited permeation inside the crystals and also by the affinity of the protein to the pendent group on the ZIF-8 surface. The polar nature of BSA not only supported adsorption on the solid surface, but also enhanced the affinity of crystal spheres through weak coordination interactions with the ZIF-8 framework. The novel approach tested in this study was therefore successful in achieving protein encapsulation with porous, biocompatible, and decomposable microcrystalline ZIF-8. The presence of both BSA and FITC-BSA in ZIF-8 was confirmed consistently by spectroscopy as well as optical and electron microscopy.
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