1. Reversible and Quantitative Photoregulation of Target Proteins
Sitao Xie, Liping Qiu, Liang Cui, Honglin Liu, Yang Sun, Hao Liang, Ding Ding, Lei He, Huixia Liu, Jiani Zhang, Zhou Chen, Xiaobing Zhang, Weihong Tan 
Chem 
Volume 3, Issue 6, Pages (December 2017)
DOI: /j.chempr
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2. Chem 2017 3, DOI: ( /j.chempr )
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3. Figure 1
Feasibility of Forming High-Order Protein Assembly for Inhibition of Thrombin Activity
(A) Real-time light-scattering spectra of mixtures containing fibrinogen (1.14 μM) and thrombin (2.5 nM) treated with different amounts of TBA-AuNPs.
(B) Real-time light-scattering spectra of mixtures containing fibrinogen (1.14 μM) and thrombin (2.5 nM) treated with 0.125 nM AuNPs (a), 0.125 nM rDNA29-AuNPs (b), 400 nM TBA (c), and 0.125 nM TBA-AuNPs (d).
(C–E) AFM characterization of thrombin only (C), the mixture of thrombin and rDNA29-Au NPs (D), and the mixture of thrombin and TBA-AuNPs (E).
Chem 2017 3, DOI: ( /j.chempr )
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4. Figure 2
Light-Driven Conformational Switch of Aptamer/AZO Probe on the Surface of AuNPs
(A) Schematic illustration of light-driven conformational switch of TBA-AZOn-AuNPs.
(B) Fluorescence changes (λem = 520 nm) of TBA-AZO3-AuNPs (a), TBA-AZO4-AuNPs (b), and TBA-AZO5-AuNPs (c) in response to light irradiation for different lengths of time.
(C) Reversible probe conformational switch of TBA-AZO4-AuNPs in response to alternating irradiation by UV (10 min) and visible light (5 min). The corresponding concentration of cTBA was 400 nM.
Chem 2017 3, DOI: ( /j.chempr )
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5. Figure 3 Visible-Light-Induced Thrombin Activation
The kinetic light-scattering spectra of samples containing fibrinogen (1.14 μM), thrombin (2.5 nM), and TBA-AZO4-AuNPs (0.125 nM) pretreated with visible light for different lengths of time.
Chem 2017 3, DOI: ( /j.chempr )
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6. Figure 4
Kinetic Fluorescence Imaging of the Reaction Process Catalyzed by Thrombin under Different Conditions
(A) Thrombin only.
(B) Thrombin treated with pretreated (UV 10 min) TBA-AZO4-AuNPs.
(C) Thrombin treated with pretreated (UV 10 min → visible 5 min) TBA-AZO4-AuNPs.
(D) Thrombin treated with pretreated (UV 10 min → visible 5 min → UV 10 min) TBA-AZO4-AuNPs.
All 3D projections of z stack images were obtained at the time point of 66 min.
Chem 2017 3, DOI: ( /j.chempr )
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7. Figure 5 Quantitative Photoregulation of Thrombin Activity
(A) Kinetic light-scattering spectra of the samples catalyzed with thrombin only (control), thrombin treated with UV-pretreated TBA-AZO4-AuNPs (a), and thrombin treated with UV-pretreated TBA-AZO4-AuNPs with visible-light irradiation applied at three kinetic catalysis reaction points (100, 200, and 300 s) (b and c).
(B) Corresponding initial catalysis reaction rates (V0) from (A).
(C) The concentration and ratio of activated thrombin under different visible treatments.
(D) Relationship between the molecular number of visible-activated thrombin per AuNP and visible illumination time.
All data in (C) and (D) were collected from three independent experiments. Error bars represent standard deviations.
Chem 2017 3, DOI: ( /j.chempr )
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8. Figure 6 Photoregulation of Blood Clotting Time of Human Plasma
(A) Linear relationship between TCT and the concentration of UV-pretreated (10 min) TBA-AZO4-AuNPs.
(B) Reversible regulation of TCT by TBA-AZO4-AuNPs in response to alternating UV- and visible-light irradiation.
All data were collected from three independent experiments. Error bars represent standard deviations.
Chem 2017 3, DOI: ( /j.chempr )
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9. Figure 7
Photoregulation of Lysozyme Activity in a Living B. subtilis System
(A) Schematic illustration of photoregulation of lysozyme activity in a living B. subtilis system.
(B) Fluorescence imaging of living B. subtilis treated with LA-AZO5-AuNP-captured lysozymes irradiated by visible light for 0 min (a), 1 min (b), 2 min (c), and 5 min (d). The concentration of lysozyme and LA-AZO5-AuNPs was 1,200 U/(mg·mL) and 10 nM, respectively. All the images were obtained 20 min after visible-light irradiation. Scale bar represents 10 μm.
(C) Relationship between the percentage of dead B. subtilis and visible illumination time. All data were collected from three independent experiments. Error bars represent standard deviations.
Chem 2017 3, DOI: ( /j.chempr )
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10. Scheme 1
Schematic Illustration of the Aptamer/AZO-Based Nanoplatform for Reversible and Quantitative Manipulation of Protein
Protein-specific aptamers modified with several light-responsive molecules are functionalized onto the surface of nanoparticles. By adjusting light irradiation, the light-responsive molecules can drive the conformational switch of aptamer between the blocked status and liberated status. In this way, the target proteins are captured around the nanoparticle or released into the medium, thus leading to inhibition or activation of the protein, respectively. Moreover, by modulating light irradiation, protein activity can be quantitatively controlled.
Chem 2017 3, DOI: ( /j.chempr )
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