期刊
ACS NANO
卷 6, 期 9, 页码 7584-7594出版社
AMER CHEMICAL SOC
DOI: 10.1021/nn302024t
关键词
protein assembly; hollow capsules; noncovalent interactions; biofunctionalization; isobutyramide graft
类别
资金
- Australian Research Council under the Discovery scheme
- Australian Research Council under Federation Fellowship scheme
We report the sequential assembly of proteins via the alternating physical adsorption of human serum albumin (HSA) and chemical grafting with isobutyramide (IBAM) or bromoisobutyramide (BrIBAM) groups. This approach, performed on silica template particles, leads to the formation of noncovalent protein films with controlled growth at the nanometer scale. Further, after template removal, hollow protein capsules with tunable wall thicknesses and high mechanical stability are obtained. The use of BrIBAM, compared to IBAM grafts, leads to significantly thicker capsule walls, highlighting the influence of the bromine atoms in the assembly process, which is discussed in terms of a theoretical model of noncovalent interactions. Another feature of the process is the possibility to functionalize the HSA capsules with other biologically active macromolecules, including enzymes, polysaccharides, or DNA plasmids, demonstrating the versatility of this approach. We also report that BrIBAM-HSA and IBAM-HSA capsules display negligible cytotoxicity in vitro with Hela cells and that their cellular uptake is dependent on the thickness of the capsule walls. These findings support the potential use of these protein capsules in tailored biological applications such as drug delivery.
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