Source 1primary paper2020MED
Toolkit/optogenetic Amyloid-b2 peptide
optogenetic Amyloid-b2 peptide
Also known as: Ab2-CRY2-mCherry, fluorescently tagged, optogenetic Amyloid-b2 peptide
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The optogenetic Amyloid-β2 peptide is a fluorescently tagged construct, also referred to as Aβ2-CRY2-mCherry, designed for blue-light-controlled oligomerization of an amyloid-β species in vivo. It enables inducible amyloid-β oligomerization for neurodegeneration-related studies.
Usefulness & Problems
Why this is useful
This tool is useful for experimentally controlling amyloid-β oligomerization with light rather than relying only on constitutive expression. In the cited study, it was applied in Drosophila, Caenorhabditis elegans, and Danio rerio to examine how amyloid-β expression and induced oligomerization affect lifespan and healthspan.
Source:
Using Drosophila, C. elegans, and D. rerio, the study reports that both Amyloid-b2 expression and induced oligomerization were detrimental to lifespan and healthspan.
Source:
The study developed a fluorescently tagged optogenetic Amyloid-b2 peptide that rapidly oligomerizes in the presence of blue light.
Problem solved
It addresses the problem of inducing amyloid-β oligomerization in a temporally controlled manner in living organisms. The reported application used this capability to distinguish effects associated with amyloid-β expression from those associated with induced oligomerization in neurodegeneration models.
Source:
Using Drosophila, C. elegans, and D. rerio, the study reports that both Amyloid-b2 expression and induced oligomerization were detrimental to lifespan and healthspan.
Source:
The study developed a fluorescently tagged optogenetic Amyloid-b2 peptide that rapidly oligomerizes in the presence of blue light.
Problem links
difficulty separating biological effects of soluble versus aggregated Amyloid-b2 peptides in vivo
LiteratureIt addresses the difficulty of separating effects caused by Amyloid-b2 expression alone from effects caused by induced oligomerization in vivo.
Source:
It addresses the difficulty of separating effects caused by Amyloid-b2 expression alone from effects caused by induced oligomerization in vivo.
Published Workflows
Objective: Develop and apply an optogenetic in vivo Amyloid-b2 model to distinguish effects of Amyloid-b2 expression from effects of acute oligomerization and to study how intracellular Amyloid-b2 oligomers contribute to neurodegenerative pathology.
Why it works: The workflow is expected to work because the engineered Amyloid-b2 peptide oligomerizes rapidly under blue light, allowing induced oligomerization to be compared against expression alone in living tissues.
intracellular Amyloid-b2 oligomer formationseparation of metabolic damage from physical damageoptogenetic inductionfluorescent taggingcomparative in vivo phenotyping across model organisms
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A reusable architecture pattern for arranging parts into an engineered system.
Techniques
No technique tags yet.
Target processes
No target processes tagged yet.
Input: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: actuator
The construct is described as Aβ2-CRY2-mCherry, indicating domain fusion of an amyloid-β2 peptide module with the CRY2 optogenetic module and an mCherry fluorescent tag. Blue light is the input modality, but the supplied evidence does not specify illumination parameters, expression strategy, or additional cofactors.
The supplied evidence is limited to a single 2020 study and provides little quantitative performance information such as kinetics, reversibility, light dose requirements, or oligomer stoichiometry. The available evidence also does not describe cell-type specificity, subcellular targeting, or validation beyond detrimental effects on lifespan and healthspan.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Using Drosophila, C. elegans, and D. rerio, the study reports that both Amyloid-b2 expression and induced oligomerization were detrimental to lifespan and healthspan.
Using Drosophila, C. elegans, and D. rerio, the study reports that both Amyloid-b2 expression and induced oligomerization were detrimental to lifespan and healthspan.
Using Drosophila, C. elegans, and D. rerio, the study reports that both Amyloid-b2 expression and induced oligomerization were detrimental to lifespan and healthspan.
Using Drosophila, C. elegans, and D. rerio, the study reports that both Amyloid-b2 expression and induced oligomerization were detrimental to lifespan and healthspan.
Using Drosophila, C. elegans, and D. rerio, the study reports that both Amyloid-b2 expression and induced oligomerization were detrimental to lifespan and healthspan.
Using Drosophila, C. elegans, and D. rerio, the study reports that both Amyloid-b2 expression and induced oligomerization were detrimental to lifespan and healthspan.
Using Drosophila, C. elegans, and D. rerio, the study reports that both Amyloid-b2 expression and induced oligomerization were detrimental to lifespan and healthspan.
Using Drosophila, C. elegans, and D. rerio, the study reports that both Amyloid-b2 expression and induced oligomerization were detrimental to lifespan and healthspan.
Physical damage caused by Amyloid-b2 oligomers recapitulated catastrophic tissue loss described as a hallmark of late Alzheimer's disease.
Physical damage caused by Amyloid-b2 oligomers recapitulated catastrophic tissue loss described as a hallmark of late Alzheimer's disease.
Physical damage caused by Amyloid-b2 oligomers recapitulated catastrophic tissue loss described as a hallmark of late Alzheimer's disease.
Physical damage caused by Amyloid-b2 oligomers recapitulated catastrophic tissue loss described as a hallmark of late Alzheimer's disease.
Physical damage caused by Amyloid-b2 oligomers recapitulated catastrophic tissue loss described as a hallmark of late Alzheimer's disease.
Physical damage caused by Amyloid-b2 oligomers recapitulated catastrophic tissue loss described as a hallmark of late Alzheimer's disease.
Physical damage caused by Amyloid-b2 oligomers recapitulated catastrophic tissue loss described as a hallmark of late Alzheimer's disease.
Physical damage caused by Amyloid-b2 oligomers recapitulated catastrophic tissue loss described as a hallmark of late Alzheimer's disease.
The optogenetic Amyloid-b2 system enabled separation of metabolic and physical damage caused by light-induced Amyloid-b2 oligomerization from damage caused by Amyloid-b2 expression alone.
The optogenetic Amyloid-b2 system enabled separation of metabolic and physical damage caused by light-induced Amyloid-b2 oligomerization from damage caused by Amyloid-b2 expression alone.
The optogenetic Amyloid-b2 system enabled separation of metabolic and physical damage caused by light-induced Amyloid-b2 oligomerization from damage caused by Amyloid-b2 expression alone.
The optogenetic Amyloid-b2 system enabled separation of metabolic and physical damage caused by light-induced Amyloid-b2 oligomerization from damage caused by Amyloid-b2 expression alone.
The optogenetic Amyloid-b2 system enabled separation of metabolic and physical damage caused by light-induced Amyloid-b2 oligomerization from damage caused by Amyloid-b2 expression alone.
The optogenetic Amyloid-b2 system enabled separation of metabolic and physical damage caused by light-induced Amyloid-b2 oligomerization from damage caused by Amyloid-b2 expression alone.
The optogenetic Amyloid-b2 system enabled separation of metabolic and physical damage caused by light-induced Amyloid-b2 oligomerization from damage caused by Amyloid-b2 expression alone.
The optogenetic Amyloid-b2 system enabled separation of metabolic and physical damage caused by light-induced Amyloid-b2 oligomerization from damage caused by Amyloid-b2 expression alone.
The results present a model that separates different aspects of disease progression.
The results present a model that separates different aspects of disease progression.
The results present a model that separates different aspects of disease progression.
The results present a model that separates different aspects of disease progression.
The results present a model that separates different aspects of disease progression.
The results present a model that separates different aspects of disease progression.
The results present a model that separates different aspects of disease progression.
The results present a model that separates different aspects of disease progression.
Li+ treatment reduced the lifespan deficit induced by Amyloid-b2 oligomers.
Li+ treatment reduced the lifespan deficit induced by Amyloid-b2 oligomers.
Li+ treatment reduced the lifespan deficit induced by Amyloid-b2 oligomers.
Li+ treatment reduced the lifespan deficit induced by Amyloid-b2 oligomers.
Li+ treatment reduced the lifespan deficit induced by Amyloid-b2 oligomers.
Li+ treatment reduced the lifespan deficit induced by Amyloid-b2 oligomers.
Li+ treatment reduced the lifespan deficit induced by Amyloid-b2 oligomers.
Li+ treatment reduced the lifespan deficit induced by Amyloid-b2 oligomers.
The study developed a fluorescently tagged optogenetic Amyloid-b2 peptide that rapidly oligomerizes in the presence of blue light.
The study developed a fluorescently tagged optogenetic Amyloid-b2 peptide that rapidly oligomerizes in the presence of blue light.
The study developed a fluorescently tagged optogenetic Amyloid-b2 peptide that rapidly oligomerizes in the presence of blue light.
The study developed a fluorescently tagged optogenetic Amyloid-b2 peptide that rapidly oligomerizes in the presence of blue light.
The study developed a fluorescently tagged optogenetic Amyloid-b2 peptide that rapidly oligomerizes in the presence of blue light.
The study developed a fluorescently tagged optogenetic Amyloid-b2 peptide that rapidly oligomerizes in the presence of blue light.
The study developed a fluorescently tagged optogenetic Amyloid-b2 peptide that rapidly oligomerizes in the presence of blue light.
The study developed a fluorescently tagged optogenetic Amyloid-b2 peptide that rapidly oligomerizes in the presence of blue light.
Approval Evidence
1 source6 linked approval claimsfirst-pass slug optogenetic-amyloid-b2-peptide
we developed a fluorescently tagged, optogenetic Amyloid-b2 peptide that oligomerizes rapidly in the presence of blue light
Source:
applicationsupports
Using Drosophila, C. elegans, and D. rerio, the study reports that both Amyloid-b2 expression and induced oligomerization were detrimental to lifespan and healthspan.
Source:
disease modelingsupports
Physical damage caused by Amyloid-b2 oligomers recapitulated catastrophic tissue loss described as a hallmark of late Alzheimer's disease.
Source:
mechanistic separationsupports
The optogenetic Amyloid-b2 system enabled separation of metabolic and physical damage caused by light-induced Amyloid-b2 oligomerization from damage caused by Amyloid-b2 expression alone.
Source:
novel modelsupports
The results present a model that separates different aspects of disease progression.
Source:
perturbation responsesupports
Li+ treatment reduced the lifespan deficit induced by Amyloid-b2 oligomers.
Source:
tool developmentsupports
The study developed a fluorescently tagged optogenetic Amyloid-b2 peptide that rapidly oligomerizes in the presence of blue light.
Source:
Comparisons
Source-stated alternatives
The abstract contrasts induced oligomerization with Amyloid-b2 expression alone. Upstream source discovery also points to extracellular Amyloid-b2 models as related but distinct alternatives.
Source:
The abstract contrasts induced oligomerization with Amyloid-b2 expression alone. Upstream source discovery also points to extracellular Amyloid-b2 models as related but distinct alternatives.
Source-backed strengths
The construct reportedly oligomerizes rapidly in response to blue light and includes an mCherry fluorescent tag, supporting optical control together with visualization. Its application across Drosophila, C. elegans, and D. rerio indicates cross-organism in vivo use, and the study reports that both expression and induced oligomerization were detrimental to lifespan and healthspan.
Compared with optogenetic probes
optogenetic Amyloid-b2 peptide and optogenetic probes address a similar problem space.
Shared frame: same top-level item type; same primary input modality: light
Compared with optogenetic zebrafish ALS model
optogenetic Amyloid-b2 peptide and optogenetic zebrafish ALS model address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: oligomerization; same primary input modality: light
Compared with organoid fusion
optogenetic Amyloid-b2 peptide and organoid fusion address a similar problem space.
Shared frame: same top-level item type; same primary input modality: light
Ranked Citations
- 1.