Source 1primary paper2018Biosensors and Bioelectronics
Toolkit/azobenzene peptide backbone photoswitch
azobenzene peptide backbone photoswitch
Also known as: azobenzene photoswitch
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
An azobenzene photoswitch incorporated into the peptide backbone allows reversible switching between a trans photostationary state devoid of secondary structure, and a cis photostationary state possessing a well-defined antiparallel β-strand geometry.
Usefulness & Problems
No literature-backed usefulness or problem-fit explainer has been materialized for this record yet.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
light-gated state-dependent protein bindingphotoisomerizationreversible conformational switchingTechniques
No technique tags yet.
Target processes
No target processes tagged yet.
Input: Light
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Observations
successCell-freeapplication demo
electrochemical impedance spectroscopy
Inferred from claim claim_4 during normalization. The probe in its random trans photostationary state does not bind α-syntrophin. Derived from claim claim_4.
Source:
Supporting Sources
Ranked Claims
Electrochemical impedance spectroscopy detected binding between the gold electrode-bound peptide in its cis photostationary state and α-syntrophin across a wide range of concentrations.
target concentration range wide range of concentrations
An azobenzene photoswitch incorporated into the peptide backbone enables reversible switching between a trans state lacking secondary structure and a cis state with antiparallel β-strand geometry.
The biosensor has high thermal stability of the cis photostationary state and enables regenerable on-off control of binding using light.
The probe in its random trans photostationary state does not bind α-syntrophin.
A light-driven photoswitchable peptide-based biosensor modeled on the nNOS β-finger was used to detect and control interaction with α-syntrophin.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug azobenzene-peptide-backbone-photoswitch
An azobenzene photoswitch incorporated into the peptide backbone allows reversible switching between a trans photostationary state devoid of secondary structure, and a cis photostationary state possessing a well-defined antiparallel β-strand geometry.
Source:
mechanismsupports
An azobenzene photoswitch incorporated into the peptide backbone enables reversible switching between a trans state lacking secondary structure and a cis state with antiparallel β-strand geometry.
Source:
performance propertysupports
The biosensor has high thermal stability of the cis photostationary state and enables regenerable on-off control of binding using light.
Source:
specificity state dependencesupports
The probe in its random trans photostationary state does not bind α-syntrophin.
Source:
Comparisons
No literature-backed comparison notes have been materialized for this record yet.
Ranked Citations
- 1.