Source 1primary paper2020UNC Libraries
Toolkit/solid-phase competitive binding assay
solid-phase competitive binding assay
Also known as: solid-phase competitive binding assays
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The solid-phase competitive binding assay is an in vitro binding assay used to test whether α-integrin cytoplasmic tails compete for association with CIB1. In the cited 2020 study, it supported the conclusion that multiple α-integrin tails can compete with the αIIb cytoplasmic tail for a shared CIB1-binding site.
Usefulness & Problems
Why this is useful
This assay is useful for functionally assessing whether distinct α-integrin cytoplasmic tails engage overlapping binding determinants on CIB1 under controlled in vitro conditions. It helps connect structural and thermodynamic observations to direct competition behavior in a solid-phase format.
Problem solved
It addresses the problem of determining whether CIB1 promiscuity toward multiple α-integrin tails reflects binding to a common site rather than independent nonoverlapping interactions. Specifically, it was used to test competition with the αIIb cytoplasmic tail for CIB1 binding.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Mechanisms
competitive bindingcompetitive bindingprotein-peptide binding mediated by hydrophobic interactionsprotein-peptide binding mediated by hydrophobic interactionsTechniques
Functional AssayTarget processes
No target processes tagged yet.
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenoperating role: sensorswitch architecture: multi component
The available evidence indicates a solid-phase competitive binding format involving CIB1 and α-integrin cytoplasmic tails, including αIIb as a reference competitor. No further practical details on immobilization strategy, detection chemistry, protein source, peptide design, or buffer conditions are provided in the supplied evidence.
The supplied evidence only establishes use as an in vitro solid-phase competition assay and does not provide quantitative performance metrics, sensitivity, throughput, or protocol details. Independent replication and validation outside the cited study are not documented in the provided evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Binding between CIB1 and α-integrin cytoplasmic tails is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Isothermal titration calorimetry measurements indicated that this binding is driven by hydrophobic interactions and depends on residues in the CIB1 consensus binding site.
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Docking models predicted that multiple α-integrin cytoplasmic tails can bind the same hydrophobic binding pocket on CIB1.
We predicted that multiple α-integrin CTs were capable of binding to the same hydrophobic binding pocket on CIB1 with docking models generated by all-atom replica exchange discrete molecular dynamics.
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Key residues in the CIB1 binding site on αIIb are well conserved across α-integrin cytoplasmic tails, enabling delineation of a consensus binding site I/L-x-x-x-L/M-W/Y-K-x-G-F-F.
A sequence alignment of all α-integrin CTs revealed that key residues in the CIB1 binding site on αIIb are well-conserved, and was used to delineate a consensus binding site (I/L-x-x-x-L/M-W/Y-K-x-G-F-F).
Approval Evidence
1 source1 linked approval claimfirst-pass slug solid-phase-competitive-binding-assay
solid-phase competitive binding assays
Source:
competitive bindingsupports
Other α-integrin cytoplasmic tails compete with the αIIb cytoplasmic tail for binding to CIB1 in vitro.
solid-phase competitive binding assays showing that other α-integrin CTs compete with the αIIb CT for binding to CIB1 in vitro
Source:
Comparisons
Source-backed strengths
The assay provided direct in vitro evidence that other α-integrin cytoplasmic tails compete with the αIIb tail for CIB1 binding. Its interpretation is consistent with reported hydrophobic interaction dependence and with docking models predicting use of the same hydrophobic pocket on CIB1.
Compared with Field-domain rapid-scan EPR at 240 GHz
solid-phase competitive binding assay and Field-domain rapid-scan EPR at 240 GHz address a similar problem space.
Shared frame: same top-level item type
Compared with fluorescence line narrowing
solid-phase competitive binding assay and fluorescence line narrowing address a similar problem space.
Shared frame: same top-level item type
Compared with native green gel system
solid-phase competitive binding assay and native green gel system address a similar problem space.
Shared frame: same top-level item type
Strengths here: looks easier to implement in practice.
Ranked Citations
- 1.