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Time-encoded bio-fluorochromic supramolecular co-assembly for rewritable security printing.

ABSTRACT: Innovative fluorescence security technologies for paper-based information are still highly pursued nowadays because data leakage and indelibility have become serious economic and social problems. Herein, we report a novel transient bio-fluorochromic supramolecular co-assembly mediated by a hydrolytic enzyme (ALP: alkaline phosphatase) towards rewritable security printing. A co-assembly based on the designed tetrabranched cationic diethynylanthracene monomer tends to be formed by adding adenosine triphosphate (ATP) as the biofuel. The resulting co-assembly possesses a time-encoded bio-fluorochromic feature, upon successively hydrolyzing ATP with ALP and re-adding new batches of ATP. On this basis, the dynamic fluorescent properties of this time-encoded co-assembly system have been successfully enabled in rewritable security patterns via an inkjet printing technique, providing fascinating potential for fluorescence security materials with a biomimetic mode.

SUBMITTER: Gao Z

PROVIDER: S-EPMC8317669 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature

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Time-encoded bio-fluorochromic supramolecular co-assembly for rewritable security printing.

Gao Zhao Z Qiu Shuai S Yan Fei F Zhang Shuyi S Wang Feng F Tian Wei W

Chemical science 20210701 29

Innovative fluorescence security technologies for paper-based information are still highly pursued nowadays because data leakage and indelibility have become serious economic and social problems. Herein, we report a novel transient bio-fluorochromic supramolecular co-assembly mediated by a hydrolytic enzyme (ALP: alkaline phosphatase) towards rewritable security printing. A co-assembly based on the designed tetrabranched cationic diethynylanthracene monomer tends to be formed by adding adenosine ...[more]

PMID: 34377397

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Project description:Supramolecular assembly of biomolecules/macromolecules stems from the desire to mimic complex biological structures and functions of living organisms. While DNA nanotechnology is already in an advanced stage, protein assembly is still in its infancy as it is a significantly difficult task due to their large molecular weight, conformational complexity and structural instability towards variation in temperature, pH or ionic strength. This article reports highly stable redox-responsive supramolecular assembly of a protein Bovine serum albumin (BSA) which is functionalized with a supramolecular structure directing unit (SSDU). The SSDU consists of a benzamide functionalized naphthalene-diimide (NDI) chromophore which is attached with the protein by a bio-reducible disulfide linker. The SSDU attached protein (NDI-BSA) exhibits spontaneous supramolecular assembly in water by off-set π-stacking among the NDI chromophores, leading to the formation of spherical nanoparticles (diameter: 150-200 nm). The same SSDU when connected with a small hydrophilic wedge (NDI-1) instead of the large globular protein, exhibits a different π-stacking mode with relatively less longitudinal displacement which results in a fibrillar network and hydrogelation. Supramolecular co-assembly of NDI-BSA and NDI-1 (3 : 7) produces similar π-stacking and an entangled 1D morphology. Both the spherical assembly of NDI-BSA or the fibrillar co-assembly of NDI-BSA + NDI-1 (3 : 7) provide sufficient thermal stability to the protein as its thermal denaturation could be completely surpassed while the secondary structure remained intact. However, the esterase like activity of the protein reduced significantly as a result of such supramolecular assembly indicating limited access by the substrate to the active site of the enzyme located in the confined environment. In the presence of glutathione (GSH), a biologically important tri-peptide, due to the cleavage of the disulfide bond, the protein became free and was released, resulting in fully regaining its enzymatic activity. Such supramolecular assembly provided excellent protection to the protein against enzymatic hydrolysis as the relative hydrolysis was estimated to be <30% for the co-assembled protein with respect to the free protein under identical conditions. Similar to bioactivity, the enzymatic hydrolysis also became prominent after GSH-treatment, confirming that the lack of hydrolysis in the supramolecularly assembled state is indeed related to the confinement of the protein in the nanostructure assembly.

Dataset Information

Time-encoded bio-fluorochromic supramolecular co-assembly for rewritable security printing.

Publications

Time-encoded bio-fluorochromic supramolecular co-assembly for rewritable security printing.

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