Source 1primary paper2023ACS Chemical Biology
Toolkit/NS3-peptide drug-displaceable complex
NS3-peptide drug-displaceable complex
Also known as: NS3-peptide complexes
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The NS3-peptide drug-displaceable complex is a chemical control system built from catalytically inactive viral NS3 protease and genetically encoded antiviral peptides that bind with high affinity. FDA-approved antiviral drugs displace the peptide from NS3 to regulate transcription, cell signaling, split-protein complementation, and recombination-related functions.
Usefulness & Problems
Why this is useful
This system provides a genetically encoded, drug-responsive way to control diverse protein activities using clinically relevant small molecules. The reported scope includes transcriptional regulation, signaling control, split-protein complementation, and orthogonal recombination tools in eukaryotic cells, with function also reported in divergent organisms to control prokaryotic recombinase activity.
Source:
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Problem solved
It addresses the need for a modular chemical switch that can control engineered protein functions through reversible disruption of a defined protein-peptide complex. The cited work specifically presents this system as a new mechanism for allosteric regulation of Cre recombinase while also extending chemical control to other cellular outputs.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
allosteric regulationhigh-affinity protein-peptide bindingsmall-molecule displacement of a protein-peptide complexTechniques
No technique tags yet.
Target processes
recombinationsignalingtranscriptionInput: Chemical
Implementation Constraints
Implementation requires expression of catalytically inactive NS3 protease together with genetically encoded antiviral peptide ligands arranged in domain-fusion architectures appropriate to the target output. Control is achieved by addition of FDA-approved drugs that displace the NS3-peptide complex, but the provided evidence does not include construct layouts, delivery methods, or cofactor requirements.
The supplied evidence does not provide quantitative performance metrics such as binding constants, drug dose-response ranges, switching kinetics, dynamic range, or leakiness. It also does not specify which FDA-approved drugs, NS3 variant, peptide sequences, or organismal contexts were tested beyond the stated functional categories.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
Allosteric Cre regulation with NS3 ligands enables orthogonal recombination tools in eukaryotic cells and functions in divergent organisms to control prokaryotic recombinase activity.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The developed NS3-ligand system provides a new mechanism to allosterically regulate Cre recombinase.
With our developed system, we invented a new mechanism to allosterically regulate Cre recombinase.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
Approval Evidence
1 source2 linked approval claimsfirst-pass slug ns3-peptide-drug-displaceable-complex
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides. Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs
Source:
drug displacement controlsupports
NS3-peptide complexes can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Through our approach, we create NS3-peptide complexes that can be displaced by FDA-approved drugs to modulate transcription, cell signaling, and split-protein complementation.
Source:
toolkit expansionsupports
The study expands the NS3-based chemical control toolkit by using catalytically inactive NS3 protease as a high-affinity binder to genetically encoded antiviral peptides.
Here, we expand the toolkit by utilizing catalytically inactive NS3 protease as a high affinity binder to genetically encoded, antiviral peptides.
Source:
Comparisons
Source-backed strengths
The core interaction uses catalytically inactive NS3 protease as a high-affinity binder for genetically encoded antiviral peptides, enabling compact multi-component control architectures. Reported applications span transcription, cell signaling, split-protein complementation, and allosteric Cre regulation, and the system is described as functioning in eukaryotic cells and in divergent organisms for control of prokaryotic recombinase activity.
Ranked Citations
- 1.