Design of photocontrolled biomolecules based on azobenzene derivatives

Zatsepin, Timofei S.; Abrosimova, L. A.; Monakhova, Mayya V.; Hiền, Lê Thị Thu; Pingoud, Alfred; Кубарева, Е. А.; Oretskaya, Tatiana S.

doi:10.1070/rc2013v082n10abeh004355

Cited by 13 publications

(16 citation statements)

References 120 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…[12][13][14][15] More complex structural processes induced by that concept include the folding/unfolding transition of relatively large proteins, 16,17 the modulation of enzymatic activity, [18][19][20] cell-cell adhesion, 21 or ion-channel activity. 3 In vivo applications became possible with the design of biocompatible azobenzene derivatives, e.g. in zebrafish embrios 22,23 or to control mitosis.…”

Section: Introductionmentioning

confidence: 99%

Photocontrolling Protein–Peptide Interactions: From Minimal Perturbation to Complete Unbinding

et al. 2019

View full text Add to dashboard Cite

An azobenzene-derived photoswitch has been covalently cross-linked to two sites of the Speptide in the RNase S complex in a manner that the alpha-helical content of the S-peptide reduces upon cis-to-trans isomerization of the photoswitch. Three complementary experimental techniques have been employed, isothermal titration calorimetry, circular dichroism spectroscopy and intrinsic tyrosine fluorescence quenching, to determine the binding affinity of the S-peptide to the S-protein in the two states of the photoswitch. Five mutants with the photoswitch attached to different sites of the S-peptide have been explored, with the goal to maximize the change in binding affinity upon photoswitching, and to identify the mechanisms that determine the binding affinity. With regard to the first goal, one mutant has been identified, which binds with reasonable affinity in the one state of the photoswitch, while specific binding is completely switched off in the other state. With regard to the second goal, accompanying molecular dynamics simulations combined with a quantitative structure activity relationship revealed that the alpha-helicity of the S-peptide in the binding pocket correlates surprisingly well with measured dissociation constants. Moreover, the simulations show that both configurations of all S-peptides exhibit quite well-defined structures, even in apparently disordered states.

show abstract

Section: Introductionmentioning

confidence: 99%

Photocontrolling Protein–Peptide Interactions: From Minimal Perturbation to Complete Unbinding

et al. 2019

View full text Add to dashboard Cite

show abstract

“…The easiest way to establish such control externally is the use of molecules that possess two clearly different stable conformations that can be interchanged with an external stimulus, usually light of a given wavelength. These molecules are conveniently called photoswitches; by far the most used and well‐documented photoswitches are derivatives of azobenzene …”

Section: Introductionmentioning

confidence: 99%

The Quest for Photoswitches Activated by Near‐Infrared Light: A Theoretical Study of the Photochemistry of BF₂‐Coordinated Azo Derivatives

2016

View full text Add to dashboard Cite

Recently synthesized BF2 -coordinated azo derivatives have been proposed as photoswitches that operate in the optical window (λ=600-1200 nm) for use in bioimaging applications. Herein, we have theoretically analyzed these compounds and modified some substituents to analyze which properties of the molecule govern its photochemistry. Our results compare rather well with the available experimental data, so our methodology, based on density functional theory (DFT) calculations for the ground electronic state and time-dependent-DFT for the first excited electronic state, is validated. Through systematic modification of different substituents of the parent system, we designed compounds that are predicted to operate fully within the optical window. We also analyzed several molecules for which the cis isomer is the more stable isomer, a quite unusual result for azobenzene derivatives that is a much coveted property for some applications of these photoactive molecules in pharmacology. Our results also provide insight into other properties relevant for photoswitches, such as the thermal stability of the less stable isomer and the magnitude of the gap between the wavelengths of the radiation that activates each isomerization process, which must be as large as possible to improve the yield of each photoisomerization. From a more general perspective, our results may provide a step towards the rational design of new photoswitches that fulfill a set of desired characteristics.

show abstract

“…The common method of introducing photosensitivity to biological molecules is by connection with photochromic moieties that undergo reversible changes in structure and conformation when exposed to different wavelengths of light . Azobenzene, whose trans and cis configurations can be reversibly isomerized by irradiating with UV and blue light, is one of the most commonly used photochromic moieties . As a photoswitch, azobenzene has many advantages, including ease of synthesis, fast photoisomerization, relatively high photostationary states, and photobleaching .…”

Section: Figurementioning

confidence: 99%

“…[6,7] Azobenzene, whose trans and cis configurations can be reversibly isomerized by irradiating with UV and blue light, is one of the most commonly used photochromic moieties. [8,9] As ap hotoswitch, azobenzene has many advantages,i ncluding ease of synthesis, fast photoisomerization,r elatively high photostationary states, and photobleaching. [10] Azobenzene derivatives have been used to control the structural conformation of peptides and proteins.…”

mentioning

confidence: 99%

Reversible Photocontrol of Lipase Activity by Incorporating a Photoswitch into the Lid Domain

et al. 2017

View full text Add to dashboard Cite

Photocontrol of enzymatic activity has become a helpful strategy to control biological processes. Herein, a method for the reversible photocontrol of lipase activity was developed by utilizing the conformational change of the lid structure. A bifunctional azobenzene derivative, whose trans/cis‐form photoisomerization processes could be used to control the folded and unfolded conformations of the α‐helix structure, was cross‐linked with two cysteine residues on the lid domain to achieve photocontrol of lipase activity. To screen for the optimum sites of cross‐linking, several cysteine‐replaced lipase variants were constructed. The variant C127C138 attached with a cross‐linker showed a threefold fully reversible activity change after illumination with UV and blue light. Furthermore, the structural change in the α‐helix of the lipase was confirmed by circular dichroism. This strategy could be applied for photocontrolling activity of other enzymes where an α‐helix is an important structural component.

show abstract

Design of photocontrolled biomolecules based on azobenzene derivatives

Cited by 13 publications

References 120 publications

Photocontrolling Protein–Peptide Interactions: From Minimal Perturbation to Complete Unbinding

Photocontrolling Protein–Peptide Interactions: From Minimal Perturbation to Complete Unbinding

The Quest for Photoswitches Activated by Near‐Infrared Light: A Theoretical Study of the Photochemistry of BF₂‐Coordinated Azo Derivatives

Reversible Photocontrol of Lipase Activity by Incorporating a Photoswitch into the Lid Domain

Contact Info

Product

Resources

About

Design of photocontrolled biomolecules based on azobenzene derivatives

Cited by 13 publications

References 120 publications

Photocontrolling Protein–Peptide Interactions: From Minimal Perturbation to Complete Unbinding

Photocontrolling Protein–Peptide Interactions: From Minimal Perturbation to Complete Unbinding

The Quest for Photoswitches Activated by Near‐Infrared Light: A Theoretical Study of the Photochemistry of BF2‐Coordinated Azo Derivatives

Reversible Photocontrol of Lipase Activity by Incorporating a Photoswitch into the Lid Domain

Contact Info

Product

Resources

About

The Quest for Photoswitches Activated by Near‐Infrared Light: A Theoretical Study of the Photochemistry of BF₂‐Coordinated Azo Derivatives