Source 1primary paper2020
Toolkit/OptoBinders
OptoBinders
Also known as: OptoBNDRs
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
OptoBinders (OptoBNDRs) are a class of light-sensitive protein binders exemplified by OptoMB, a light-controlled monobody. Reported OptoBinders enable reversible light-dependent modulation of protein binding affinity, including an SH2-binding OptoMB with an approximately 300-fold light-dependent affinity shift.
Usefulness & Problems
Why this is useful
OptoBinders are useful for dynamically controlling protein-protein recognition with light, allowing binding interactions to be switched without permanently altering the target protein. In the reported application, αSH2-OptoMB enabled single-step purification of SH2-tagged proteins directly from crude E. coli extract with 99.8% purity and over 40% yield.
Source:
our αSH2-OptoMB can be used to purify SH2-tagged proteins directly from crude E. coli extract, achieving 99.8% purity and over 40% yield in a single purification step
Source:
a light-controlled monobody (OptoMB) that works in vitro and in vivo , whose affinity for its SH2-domain target exhibits a 300-fold shift in binding affinity upon illumination
Problem solved
This tool addresses the problem of achieving externally controllable, reversible, and potentially target-selective protein binding. The source also states that OptoBinders have the potential to be designed as light-switchable binders of untagged proteins with high affinity and selectivity.
Source:
our αSH2-OptoMB can be used to purify SH2-tagged proteins directly from crude E. coli extract, achieving 99.8% purity and over 40% yield in a single purification step
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
light-dependent switching of protein binding affinityreversible modulation of protein-protein bindingreversible protein-protein binding modulationTechniques
Computational DesignTarget processes
No target processes tagged yet.
Input: Light
Implementation Constraints
The reported example is a monobody-based light-sensitive binder, with αSH2-OptoMB used against SH2-tagged proteins in crude E. coli extract. The provided evidence does not specify illumination wavelength, chromophore requirements, construct architecture, or delivery constraints.
The supplied evidence is centered on a single published example, OptoMB, and does not establish performance across multiple targets or binder scaffolds. The claim that OptoBinders can be designed for untagged proteins is presented as potential rather than broad experimental validation.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
αSH2-OptoMB can purify SH2-tagged proteins directly from crude E. coli extract in a single purification step with 99.8% purity and over 40% yield.
our αSH2-OptoMB can be used to purify SH2-tagged proteins directly from crude E. coli extract, achieving 99.8% purity and over 40% yield in a single purification step
purification steps 1 steppurity 99.8 %yield 40 %
αSH2-OptoMB can purify SH2-tagged proteins directly from crude E. coli extract in a single purification step with 99.8% purity and over 40% yield.
our αSH2-OptoMB can be used to purify SH2-tagged proteins directly from crude E. coli extract, achieving 99.8% purity and over 40% yield in a single purification step
purification steps 1 steppurity 99.8 %yield 40 %
αSH2-OptoMB can purify SH2-tagged proteins directly from crude E. coli extract in a single purification step with 99.8% purity and over 40% yield.
our αSH2-OptoMB can be used to purify SH2-tagged proteins directly from crude E. coli extract, achieving 99.8% purity and over 40% yield in a single purification step
purification steps 1 steppurity 99.8 %yield 40 %
αSH2-OptoMB can purify SH2-tagged proteins directly from crude E. coli extract in a single purification step with 99.8% purity and over 40% yield.
our αSH2-OptoMB can be used to purify SH2-tagged proteins directly from crude E. coli extract, achieving 99.8% purity and over 40% yield in a single purification step
purification steps 1 steppurity 99.8 %yield 40 %
αSH2-OptoMB can purify SH2-tagged proteins directly from crude E. coli extract in a single purification step with 99.8% purity and over 40% yield.
our αSH2-OptoMB can be used to purify SH2-tagged proteins directly from crude E. coli extract, achieving 99.8% purity and over 40% yield in a single purification step
purification steps 1 steppurity 99.8 %yield 40 %
αSH2-OptoMB can purify SH2-tagged proteins directly from crude E. coli extract in a single purification step with 99.8% purity and over 40% yield.
our αSH2-OptoMB can be used to purify SH2-tagged proteins directly from crude E. coli extract, achieving 99.8% purity and over 40% yield in a single purification step
purification steps 1 steppurity 99.8 %yield 40 %
αSH2-OptoMB can purify SH2-tagged proteins directly from crude E. coli extract in a single purification step with 99.8% purity and over 40% yield.
our αSH2-OptoMB can be used to purify SH2-tagged proteins directly from crude E. coli extract, achieving 99.8% purity and over 40% yield in a single purification step
purification steps 1 steppurity 99.8 %yield 40 %
OptoMB belongs to a class of light-sensitive protein binders called OptoBinders.
This OptoMB belongs to a new class of light-sensitive protein binders we call OptoBinders (OptoBNDRs)
OptoMB belongs to a class of light-sensitive protein binders called OptoBinders.
This OptoMB belongs to a new class of light-sensitive protein binders we call OptoBinders (OptoBNDRs)
OptoMB belongs to a class of light-sensitive protein binders called OptoBinders.
This OptoMB belongs to a new class of light-sensitive protein binders we call OptoBinders (OptoBNDRs)
OptoMB belongs to a class of light-sensitive protein binders called OptoBinders.
This OptoMB belongs to a new class of light-sensitive protein binders we call OptoBinders (OptoBNDRs)
OptoMB belongs to a class of light-sensitive protein binders called OptoBinders.
This OptoMB belongs to a new class of light-sensitive protein binders we call OptoBinders (OptoBNDRs)
OptoMB belongs to a class of light-sensitive protein binders called OptoBinders.
This OptoMB belongs to a new class of light-sensitive protein binders we call OptoBinders (OptoBNDRs)
OptoMB belongs to a class of light-sensitive protein binders called OptoBinders.
This OptoMB belongs to a new class of light-sensitive protein binders we call OptoBinders (OptoBNDRs)
OptoBinders have the potential to be designed to bind proteins of interest as light-switchable binders of untagged proteins with high affinity and selectivity.
OptoBinders (OptoBNDRs) which, by virtue of their ability to be designed to bind any protein of interest, have the potential to find new powerful applications as light-switchable binders of untagged proteins with high affinity and selectivity
OptoBinders have the potential to be designed to bind proteins of interest as light-switchable binders of untagged proteins with high affinity and selectivity.
OptoBinders (OptoBNDRs) which, by virtue of their ability to be designed to bind any protein of interest, have the potential to find new powerful applications as light-switchable binders of untagged proteins with high affinity and selectivity
OptoBinders have the potential to be designed to bind proteins of interest as light-switchable binders of untagged proteins with high affinity and selectivity.
OptoBinders (OptoBNDRs) which, by virtue of their ability to be designed to bind any protein of interest, have the potential to find new powerful applications as light-switchable binders of untagged proteins with high affinity and selectivity
OptoBinders have the potential to be designed to bind proteins of interest as light-switchable binders of untagged proteins with high affinity and selectivity.
OptoBinders (OptoBNDRs) which, by virtue of their ability to be designed to bind any protein of interest, have the potential to find new powerful applications as light-switchable binders of untagged proteins with high affinity and selectivity
OptoBinders have the potential to be designed to bind proteins of interest as light-switchable binders of untagged proteins with high affinity and selectivity.
OptoBinders (OptoBNDRs) which, by virtue of their ability to be designed to bind any protein of interest, have the potential to find new powerful applications as light-switchable binders of untagged proteins with high affinity and selectivity
OptoBinders have the potential to be designed to bind proteins of interest as light-switchable binders of untagged proteins with high affinity and selectivity.
OptoBinders (OptoBNDRs) which, by virtue of their ability to be designed to bind any protein of interest, have the potential to find new powerful applications as light-switchable binders of untagged proteins with high affinity and selectivity
OptoBinders have the potential to be designed to bind proteins of interest as light-switchable binders of untagged proteins with high affinity and selectivity.
OptoBinders (OptoBNDRs) which, by virtue of their ability to be designed to bind any protein of interest, have the potential to find new powerful applications as light-switchable binders of untagged proteins with high affinity and selectivity
OptoMB is a light-controlled monobody whose affinity for its SH2-domain target shifts by 300-fold upon illumination.
a light-controlled monobody (OptoMB) that works in vitro and in vivo , whose affinity for its SH2-domain target exhibits a 300-fold shift in binding affinity upon illumination
binding affinity shift upon illumination 300 fold
OptoMB is a light-controlled monobody whose affinity for its SH2-domain target shifts by 300-fold upon illumination.
a light-controlled monobody (OptoMB) that works in vitro and in vivo , whose affinity for its SH2-domain target exhibits a 300-fold shift in binding affinity upon illumination
binding affinity shift upon illumination 300 fold
OptoMB is a light-controlled monobody whose affinity for its SH2-domain target shifts by 300-fold upon illumination.
a light-controlled monobody (OptoMB) that works in vitro and in vivo , whose affinity for its SH2-domain target exhibits a 300-fold shift in binding affinity upon illumination
binding affinity shift upon illumination 300 fold
OptoMB is a light-controlled monobody whose affinity for its SH2-domain target shifts by 300-fold upon illumination.
a light-controlled monobody (OptoMB) that works in vitro and in vivo , whose affinity for its SH2-domain target exhibits a 300-fold shift in binding affinity upon illumination
binding affinity shift upon illumination 300 fold
OptoMB is a light-controlled monobody whose affinity for its SH2-domain target shifts by 300-fold upon illumination.
a light-controlled monobody (OptoMB) that works in vitro and in vivo , whose affinity for its SH2-domain target exhibits a 300-fold shift in binding affinity upon illumination
binding affinity shift upon illumination 300 fold
OptoMB is a light-controlled monobody whose affinity for its SH2-domain target shifts by 300-fold upon illumination.
a light-controlled monobody (OptoMB) that works in vitro and in vivo , whose affinity for its SH2-domain target exhibits a 300-fold shift in binding affinity upon illumination
binding affinity shift upon illumination 300 fold
OptoMB is a light-controlled monobody whose affinity for its SH2-domain target shifts by 300-fold upon illumination.
a light-controlled monobody (OptoMB) that works in vitro and in vivo , whose affinity for its SH2-domain target exhibits a 300-fold shift in binding affinity upon illumination
binding affinity shift upon illumination 300 fold
Approval Evidence
1 source2 linked approval claimsfirst-pass slug optobinders
This OptoMB belongs to a new class of light-sensitive protein binders we call OptoBinders (OptoBNDRs)
Source:
class membershipsupports
OptoMB belongs to a class of light-sensitive protein binders called OptoBinders.
This OptoMB belongs to a new class of light-sensitive protein binders we call OptoBinders (OptoBNDRs)
Source:
design potentialsupports
OptoBinders have the potential to be designed to bind proteins of interest as light-switchable binders of untagged proteins with high affinity and selectivity.
OptoBinders (OptoBNDRs) which, by virtue of their ability to be designed to bind any protein of interest, have the potential to find new powerful applications as light-switchable binders of untagged proteins with high affinity and selectivity
Source:
Comparisons
Source-backed strengths
A reported OptoBinder, OptoMB, showed a large light-dependent change in affinity of about 300-fold for an SH2-domain target. The αSH2-OptoMB application demonstrated practical utility in protein purification from crude E. coli extract, achieving 99.8% purity and over 40% yield in a single step.
Ranked Citations
- 1.