Source 1primary paper2023Current Pharmaceutical Design
Toolkit/CIB1-targeting decoy peptides
CIB1-targeting decoy peptides
Also known as: decoy peptides targeting CIB1
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
CIB1-targeting decoy peptides are computationally modeled peptide variants intended to bind calcium and integrin-binding protein 1 (CIB1) and inhibit its function. A 2023 in silico study reported that top-ranked second-generation mutant peptides had greater predicted inhibitory potential than the reference peptide UNC10245092.
Usefulness & Problems
Why this is useful
These constructs are useful as candidate CIB1 inhibitors identified through in silico mutagenesis and modeling. The reported designs aim to obscure the role of CIB1 in triple-negative breast cancer progression and to preserve or restore the tumor suppressor function associated with the reference peptide UNC10245092.
Source:
and have the potency to prevent or restore the tumor suppressor function of UNC10245092
Problem solved
This tool addresses the need to generate improved peptide inhibitors of CIB1 relative to an existing reference peptide, UNC10245092. The available evidence indicates a computational effort to identify variants with higher predicted potency against CIB1 in the context of triple-negative breast cancer.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A reusable architecture pattern for arranging parts into an engineered system.
Mechanisms
competitive inhibition by decoy peptide binding to cib1competitive inhibition of cib1 by decoy peptide bindingTechniques
Computational DesignTarget processes
No target processes tagged yet.
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationoperating role: actuator
The available evidence supports that these are peptide variants generated by in silico mutagenesis and modeling against CIB1. No details are provided on peptide sequence, expression or synthesis, construct architecture, cofactors, delivery, or assay implementation.
The evidence is limited to a single 2023 in silico study and provides no experimental biochemical, cellular, or in vivo validation. No quantitative binding data, structural validation, delivery strategy, or direct functional assay results are provided in the supplied evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide UNC10245092.
Our results indicate that among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide (UNC10245092)
Among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide UNC10245092.
Our results indicate that among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide (UNC10245092)
Among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide UNC10245092.
Our results indicate that among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide (UNC10245092)
Among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide UNC10245092.
Our results indicate that among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide (UNC10245092)
Among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide UNC10245092.
Our results indicate that among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide (UNC10245092)
Among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide UNC10245092.
Our results indicate that among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide (UNC10245092)
Among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide UNC10245092.
Our results indicate that among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide (UNC10245092)
The mutant 2nd mutants have the potency to prevent or restore the tumor suppressor function of UNC10245092.
and have the potency to prevent or restore the tumor suppressor function of UNC10245092
The mutant 2nd mutants have the potency to prevent or restore the tumor suppressor function of UNC10245092.
and have the potency to prevent or restore the tumor suppressor function of UNC10245092
The mutant 2nd mutants have the potency to prevent or restore the tumor suppressor function of UNC10245092.
and have the potency to prevent or restore the tumor suppressor function of UNC10245092
The mutant 2nd mutants have the potency to prevent or restore the tumor suppressor function of UNC10245092.
and have the potency to prevent or restore the tumor suppressor function of UNC10245092
The mutant 2nd mutants have the potency to prevent or restore the tumor suppressor function of UNC10245092.
and have the potency to prevent or restore the tumor suppressor function of UNC10245092
The mutant 2nd mutants have the potency to prevent or restore the tumor suppressor function of UNC10245092.
and have the potency to prevent or restore the tumor suppressor function of UNC10245092
The mutant 2nd mutants have the potency to prevent or restore the tumor suppressor function of UNC10245092.
and have the potency to prevent or restore the tumor suppressor function of UNC10245092
Approval Evidence
1 source2 linked approval claimsfirst-pass slug cib1-targeting-decoy-peptides
In silico Mutagenesis and Modeling of Decoy Peptides Targeting CIB1
Source:
comparative activitysupports
Among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide UNC10245092.
Our results indicate that among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide (UNC10245092)
Source:
functional potentialsupports
The mutant 2nd mutants have the potency to prevent or restore the tumor suppressor function of UNC10245092.
and have the potency to prevent or restore the tumor suppressor function of UNC10245092
Source:
Comparisons
Source-backed strengths
The main reported strength is that top selected second-generation mutant peptides were predicted to inhibit CIB1 more effectively than UNC10245092. The study also reported predicted potential for these mutants to prevent or restore the tumor suppressor function attributed to UNC10245092.
Source:
Our results indicate that among the top five selected peptides, the mutant 2nd mutants have more potential to inhibit CIB1 than the reference peptide (UNC10245092)
Compared with mMORp
CIB1-targeting decoy peptides and mMORp address a similar problem space.
Shared frame: same top-level item type
Strengths here: looks easier to implement in practice.
Compared with self-complementary AAV genomes
CIB1-targeting decoy peptides and self-complementary AAV genomes address a similar problem space.
Shared frame: same top-level item type
Compared with split-ring metamaterial sensor with luxuriant gaps
CIB1-targeting decoy peptides and split-ring metamaterial sensor with luxuriant gaps address a similar problem space.
Shared frame: same top-level item type
Ranked Citations
- 1.