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Design, Synthesis, Investigation, and Application of a Macromolecule Photoswitch.

ABSTRACT: Azobenzene (AZO) has attracted increasing interest due to its reversible structural change upon a light stimulus. However, poor fatigue durability and the photobleaching phenomenon restricts its further application. Herein, the AZO domain as a pendent group, was incorporated into copolymers, which was synthesized by radical copolymerization in the research. Structure-properties of synthesized copolymer can be adjusted by monomer ratios. Emphatically, responsive properties of copolymer in different solutions were investigated. In the DMSO solution, copolymer exhibited effective structural change, stable rapid responsive time (1 min) upon UV light at room temperature, stable relative acceptable recovery time (100 min) upon white light at room temperature, and good fatigue resistance property. In an aqueous solution, even more controllable responsive properties and fatigue resistance properties for copolymer were verified by results. More pervasively, the recovery process could be controlled by light density and temperature. In order to clarify reasons for the difference between the AZO molecule and the AZO domain of copolymer, energy barrier or interactions between single atoms or even structural units was calculated using the density functional theory (DFT). Furthermore, the status of copolymer was characterized by dynamic light scattering (DLS) and transmission electron microscope (TEM). Finally, copolymer was further functionalized with bioactive protein (concanavalin, ConA) to reduce the cytotoxicity of the AZO molecule.

SUBMITTER: Pang J

PROVIDER: S-EPMC6403147 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature

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Design, Synthesis, Investigation, and Application of a Macromolecule Photoswitch.

Pang Juan J Gao Ziyu Z Tan Huaping H Mao Xincheng X Wang Huiming H Hu Xiaohong X

Frontiers in chemistry 20190228

Azobenzene (AZO) has attracted increasing interest due to its reversible structural change upon a light stimulus. However, poor fatigue durability and the photobleaching phenomenon restricts its further application. Herein, the AZO domain as a pendent group, was incorporated into copolymers, which was synthesized by radical copolymerization in the research. Structure-properties of synthesized copolymer can be adjusted by monomer ratios. Emphatically, responsive properties of copolymer in differe ...[more]

PMID: 30873401

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Project description:Upon blue light irradiation, photoactive yellow protein (PYP) undergoes a conformational change that involves large movements at the N-terminus of the protein. We reasoned that this conformational change might be used to control other protein or peptide sequences if these were introduced as linkers connecting the N- and C-termini of PYP in a circular permutant. For such a design strategy to succeed, the circularly permuted PYP (cPYP) would have to fold normally and undergo a photocycle similar to that of the wild-type protein. We created a test cPYP by connecting the N- and C-termini of wild-type PYP (wtPYP) with a GGSGGSGG linker polypeptide and introducing new N- and C-termini at G115 and S114, respectively. Biophysical analysis indicated that this cPYP adopts a dark-state conformation much like wtPYP and undergoes wtPYP-like photoisomerization driven by blue light. However, thermal recovery of dark-state cPYP is ?10-fold faster than that of wtPYP, so that very bright light is required to significantly populate the light state. Targeted mutations at M121E (M100 in wtPYP numbering) were found to enhance the light sensitivity substantially by lengthening the lifetime of the light state to ?10 min. Nuclear magnetic resonance (NMR), circular dichroism, and UV-vis analysis indicated that the M121E-cPYP mutant also adopts a dark-state structure like that of wtPYP, although protonated and deprotonated forms of the chromophore coexist, giving rise to a shoulder near 380 nm in the UV-vis absorption spectrum. Fluorine NMR studies with fluorotryptophan-labeled M121E-cPYP show that blue light drives large changes in conformational dynamics and leads to solvent exposure of Trp7 (Trp119 in wtPYP numbering), consistent with substantial rearrangement of the N-terminal cap structure. M121E-cPYP thus provides a scaffold that may allow a wider range of photoswitchable protein designs via replacement of the linker polypeptide with a target protein or peptide sequence.

Dataset Information

Design, Synthesis, Investigation, and Application of a Macromolecule Photoswitch.

Publications

Design, Synthesis, Investigation, and Application of a Macromolecule Photoswitch.

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