Biological applications of zinc imidazole framework through protein encapsulationopen access
- Authors
- Kumar, Pawan; Bansal, Vasudha; Paul,Albish K.; Bharadwaj, Lalit M.; Deep, Akash; Kim, Ki-Hyun
- Issue Date
- Oct-2016
- Publisher
- SPRINGER HEIDELBERG
- Keywords
- Zeolitic imidazolate framework (ZIF-8); Proteins; BSA; Successive adsorption
- Citation
- APPLIED NANOSCIENCE, v.6, no.7, pp.951 - 957
- Indexed
- SCIE
SCOPUS
- Journal Title
- APPLIED NANOSCIENCE
- Volume
- 6
- Number
- 7
- Start Page
- 951
- End Page
- 957
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/4359
- DOI
- 10.1007/s13204-015-0511-x
- ISSN
- 2190-5509
- Abstract
- 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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