Azobenzene switch with a long-lived cis-state to photocontrol the enzyme activity of a histone deacetylase-like amidohydrolase

Korbus, Michael; Balasubramanian, Ganesh; Müller‐Plathe, Florian; Kolmar, Harald; Meyer‐Almes, Franz‐Josef

doi:10.1515/hsz-2013-0246

Cited by 13 publications

(25 citation statements)

References 43 publications

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“…HDAH variant M30C was used as conjugate and test model to investigate the AMD dependent influence on the photoswitch capability with respect to the spacer length. Both HDAH variants were generated by site-directed mutagenesis, expressed in Escherichia coli strain XL1-blue and purified as previously reported [7].…”

Section: Employed Hdah Variantsmentioning

confidence: 99%

“…The single solvent accessible cysteine of HDAH variant M30C was chemically modified by 4-PAM or AMDs (1a-e) by a 4-fold molar excess in MC buffer (supplemented with 8% DMSO) and the modification procedure continued as described previously [7].…”

Section: Modification Of Hdah Variant M30cmentioning

confidence: 99%

“…The isomerization process of light-responsive molecules offers diversified applications like photocontrol of the protein function [4][5][6][7][8] or the conformational change of protein structures [9,10] as well as protein assembly [11]. Azobenzene is the most studied light-switchable molecule.…”

Section: Introductionmentioning

confidence: 99%

“…These advantages were combined by the synthesis of a series of new azobenzenealkylmaleimides (AMDs) 1a-e. Subsequently, the reactive probes were conjugated to a specific cysteine-variant (M30C) of a photoswitchable bacterial histone deacetylase-like amidohydrolase (HDAH) from Bordetella/Alcaligenes strain FB188 [7] to investigate the influence of AMD spacer length variation as well as the cis-and trans-configuration on the photocontrol behavior of the enzyme activity. Furthermore, spatiotemporal controlled deacetylation reactions could be employed in biotechnological and biomedical applications to regulate the deacetylation of biomolecules or chemical compounds in a precise and defined manner to meet desired needs.…”

Section: Introductionmentioning

confidence: 99%

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Synthesis of azobenzenealkylmaleimide probes to photocontrol the enzyme activity of a bacterial histone deacetylase-like amidohydrolase

Horstmann

Korbus

Friedmann

et al. 2014

Bioorganic Chemistry

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Section: Employed Hdah Variantsmentioning

confidence: 99%

Section: Modification Of Hdah Variant M30cmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Synthesis of azobenzenealkylmaleimide probes to photocontrol the enzyme activity of a bacterial histone deacetylase-like amidohydrolase

Horstmann

Korbus

Friedmann

et al. 2014

Bioorganic Chemistry

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“…In a recent publication by the Meyer-Almes group (Figure 9.6), they described how they modified several alkylmaleimides of varying chain length with an azobenzene system, and then covalently attached the resulting photochromic assembly to a predetermined site on a mutant histone deacetylase-like aminohydrolase (HDAH) [52,53]. The mutant variant of HDAH (M30S) contains a maleimide-reactive cysteine along the edge of an outward facing solvent loop, adjacent to the active site of the enzyme.…”

Section: Site-selective Introduction Of Photochromic Species -Single mentioning

confidence: 99%

Photochromic Materials in Biochemistry

Wilson

Branda

2016

Photochromic Materials: Preparation, Properties and Applications

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How Photoisomerization Drives Peptide Folding and Unfolding: Insights from QM/MM and MM Dynamics Simulations

et al. 2016

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Photoswitchable azobenzene cross-linkers can control the folding and unfolding of peptides by photoisomerization and can thus regulate peptide affinities and enzyme activities.U sing quantum mechanics/molecular mechanics (QM/MM) methods and classical MM force fields,w er eport the first molecular dynamics simulations of the photoinduced folding and unfolding processes in the azobenzene crosslinked FK-11 peptide.Wefind that the interactions between the peptide and the azobenzene cross-linker are crucial for controlling the evolution of the secondary structure of the peptide and responsible for accelerating the folding and unfolding events.T hey also modify the photoisomerization mechanism of the azobenzene cross-linker compared with the situation in vacuo or in solution.Anefficient light-sensitive peptide can be constructed by cross-linking aphotoswitchable small cross-linker molecule to the peptide backbone;photoinduced structural changes of the cross-linker can trigger reversible changes in peptide conformations.T his kind of photoresponse can provide an avenue for probing and manipulating complex living systems.[1] Thep hotoinduced conformational dynamics of peptides with built-in azobenzenes has been exploited to probe functional changes of proteins,t omanipulate enzyme activities,a nd to control cell signaling.[2] However,adetailed mechanistic understanding of these processes at the atomistic level is still lacking.Experimentally,t ime-resolved infrared spectroscopy was employed to monitor the conformational dynamics of crosslinked peptides;itwas found that both folding and unfolding processes show complex spectral kinetics and strongly depend on the photoexcitation wavelength and on temperature. [3] Computationally,a zobenzene-linked peptides were explored by classical molecular dynamics (MD) simulations.[4] However,i nt hese studies,t he initial nonadiabatic photoisomerization was not considered or was only simulated using as imple model potential, and the effects of the photoisomerization on the subsequent conformational dynamics of peptides were not investigated;m oreover,o nly the photoinduced folding dynamics was simulated in those studies. [4] Theu nfolding dynamics of cross-linked peptides has rarely been explored experimentally because peptide unfolding processes are generally endothermic and difficult to study. [4f] Asalient dynamical feature of these cross-linked peptides is that their folding and unfolding processes are significantly accelerated compared with peptides without cross-linkers. [3a] This speedup must originate from the interaction between the cross-linker and the peptide.Athorough understanding of this interplay is crucial to rationalize the folding and unfolding dynamics of cross-linked peptides,t os elect appropriate cross-linkers,t ooptimize cross-linking positions,a nd eventually to control these photoinduced conformational changes. It is difficult to obtain detailed information on these interactions solely from experiment, and it is thus desirable to perform th...

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Azobenzene switch with a long-lived cis-state to photocontrol the enzyme activity of a histone deacetylase-like amidohydrolase

Cited by 13 publications

References 43 publications

Synthesis of azobenzenealkylmaleimide probes to photocontrol the enzyme activity of a bacterial histone deacetylase-like amidohydrolase

Synthesis of azobenzenealkylmaleimide probes to photocontrol the enzyme activity of a bacterial histone deacetylase-like amidohydrolase

Photochromic Materials in Biochemistry

How Photoisomerization Drives Peptide Folding and Unfolding: Insights from QM/MM and MM Dynamics Simulations

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