Source 1primary paper2020ACS Chemical Biology
Toolkit/UNC10245092
UNC10245092
Also known as: reference peptide
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
UNC10245092 is a previously identified linear peptide inhibitor that binds calcium and integrin binding protein 1 (CIB1). It has been used as a reference peptide in structural and in silico studies of CIB1-targeting decoy peptide design.
Usefulness & Problems
Why this is useful
UNC10245092 is useful as a benchmark CIB1-binding peptide for comparing newly designed inhibitors and decoy peptides. Its value is supported by the availability of a crystal structure of CIB1 in complex with the peptide, which enables structure-guided analysis of CIB1-peptide interactions.
Source:
and have the potency to prevent or restore the tumor suppressor function of UNC10245092
Source:
These studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
Problem solved
This construct helps address the problem of obtaining a defined peptide ligand for inhibiting or interrogating CIB1, a signaling-associated protein. The supplied evidence specifically supports its use as a reference standard for efforts to design improved CIB1-targeting peptides, including in the context of triple-negative breast cancer modeling studies.
Problem links
Need conditional control of signaling activity
DerivedUNC10245092 is a previously identified linear peptide inhibitor that binds calcium and integrin binding protein 1 (CIB1). It has been used as a reference peptide in structural and in silico studies of CIB1-targeting decoy peptide design.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A reusable architecture pattern for arranging parts into an engineered system.
Target processes
signalingInput: Chemical
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationoperating role: regulatorswitch architecture: uncaging
Practical implementation details are limited to its identity as a linear peptide inhibitor and the existence of a crystal structure of the CIB1-UNC10245092 complex in the Protein Data Bank. The supplied evidence does not specify expression or synthesis conditions, delivery method, cofactor requirements, or construct architecture beyond its use as a peptide reference.
The provided evidence does not report the peptide sequence, quantitative affinity, cellular activity, or in vivo efficacy of UNC10245092. Available comparative claims indicate that some later designed mutant peptides were predicted to interact more strongly with CIB1 and to have greater inhibitory potential than this reference peptide.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2021ACS Medicinal Chemistry Letters
Source 3primary paper2023Current Pharmaceutical Design
Source 4primary paper2022Research Square (Research Square)
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
Among the top five selected designed peptides, mutant 2 showed stronger interactions with CIB1 than the reference peptide UNC10245092.
Our results indicate that amongst the top five selected peptides, mutant 2 nd mutant have strong interactions with CIB1 than the reference peptide (UNC10245092)
Among the top five selected designed peptides, mutant 2 showed stronger interactions with CIB1 than the reference peptide UNC10245092.
Our results indicate that amongst the top five selected peptides, mutant 2 nd mutant have strong interactions with CIB1 than the reference peptide (UNC10245092)
Among the top five selected designed peptides, mutant 2 showed stronger interactions with CIB1 than the reference peptide UNC10245092.
Our results indicate that amongst the top five selected peptides, mutant 2 nd mutant have strong interactions with CIB1 than the reference peptide (UNC10245092)
Among the top five selected designed peptides, mutant 2 showed stronger interactions with CIB1 than the reference peptide UNC10245092.
Our results indicate that amongst the top five selected peptides, mutant 2 nd mutant have strong interactions with CIB1 than the reference peptide (UNC10245092)
Among the top five selected designed peptides, mutant 2 showed stronger interactions with CIB1 than the reference peptide UNC10245092.
Our results indicate that amongst the top five selected peptides, mutant 2 nd mutant have strong interactions with CIB1 than the reference peptide (UNC10245092)
Among the top five selected designed peptides, mutant 2 showed stronger interactions with CIB1 than the reference peptide UNC10245092.
Our results indicate that amongst the top five selected peptides, mutant 2 nd mutant have strong interactions with CIB1 than the reference peptide (UNC10245092)
Among the top five selected designed peptides, mutant 2 showed stronger interactions with CIB1 than the reference peptide UNC10245092.
Our results indicate that amongst the top five selected peptides, mutant 2 nd mutant have strong interactions with CIB1 than the reference peptide (UNC10245092)
The study aimed to design novel peptides from the reference peptide UNC10245092 to target CIB1 using residue scan methodology.
The goal of this study is to design novel peptides from the reference peptide (UNC10245092) through residue scan methodology.
The study aimed to design novel peptides from the reference peptide UNC10245092 to target CIB1 using residue scan methodology.
The goal of this study is to design novel peptides from the reference peptide (UNC10245092) through residue scan methodology.
The study aimed to design novel peptides from the reference peptide UNC10245092 to target CIB1 using residue scan methodology.
The goal of this study is to design novel peptides from the reference peptide (UNC10245092) through residue scan methodology.
The study aimed to design novel peptides from the reference peptide UNC10245092 to target CIB1 using residue scan methodology.
The goal of this study is to design novel peptides from the reference peptide (UNC10245092) through residue scan methodology.
The study aimed to design novel peptides from the reference peptide UNC10245092 to target CIB1 using residue scan methodology.
The goal of this study is to design novel peptides from the reference peptide (UNC10245092) through residue scan methodology.
The study aimed to design novel peptides from the reference peptide UNC10245092 to target CIB1 using residue scan methodology.
The goal of this study is to design novel peptides from the reference peptide (UNC10245092) through residue scan methodology.
The study aimed to design novel peptides from the reference peptide UNC10245092 to target CIB1 using residue scan methodology.
The goal of this study is to design novel peptides from the reference peptide (UNC10245092) through residue scan methodology.
The selected designed peptides were predicted to have the potency to prevent binding between RAF and CIB1.
and have the potency to prevent the binding of RAF and CIB1.
The selected designed peptides were predicted to have the potency to prevent binding between RAF and CIB1.
and have the potency to prevent the binding of RAF and CIB1.
The selected designed peptides were predicted to have the potency to prevent binding between RAF and CIB1.
and have the potency to prevent the binding of RAF and CIB1.
The selected designed peptides were predicted to have the potency to prevent binding between RAF and CIB1.
and have the potency to prevent the binding of RAF and CIB1.
The selected designed peptides were predicted to have the potency to prevent binding between RAF and CIB1.
and have the potency to prevent the binding of RAF and CIB1.
The selected designed peptides were predicted to have the potency to prevent binding between RAF and CIB1.
and have the potency to prevent the binding of RAF and CIB1.
The selected designed peptides were predicted to have the potency to prevent binding between RAF and CIB1.
and have the potency to prevent the binding of RAF and CIB1.
UNC10245131 has low nanomolar affinity for CIB1.
UNC10245131, a cyclic peptide with low nanomolar affinity
affinity low nanomolar
UNC10245131 has low nanomolar affinity for CIB1.
UNC10245131, a cyclic peptide with low nanomolar affinity
affinity low nanomolar
UNC10245131 has low nanomolar affinity for CIB1.
UNC10245131, a cyclic peptide with low nanomolar affinity
affinity low nanomolar
UNC10245131 has low nanomolar affinity for CIB1.
UNC10245131, a cyclic peptide with low nanomolar affinity
affinity low nanomolar
UNC10245131 has low nanomolar affinity for CIB1.
UNC10245131, a cyclic peptide with low nanomolar affinity
affinity low nanomolar
UNC10245131 has low nanomolar affinity for CIB1.
UNC10245131, a cyclic peptide with low nanomolar affinity
affinity low nanomolar
UNC10245131 has low nanomolar affinity for CIB1.
UNC10245131, a cyclic peptide with low nanomolar affinity
affinity low nanomolar
UNC10245131 has improved permeability and stability relative to UNC10245092.
improved permeability and stability over previously identified linear peptide inhibitor UNC10245092
UNC10245131 has improved permeability and stability relative to UNC10245092.
improved permeability and stability over previously identified linear peptide inhibitor UNC10245092
UNC10245131 has improved permeability and stability relative to UNC10245092.
improved permeability and stability over previously identified linear peptide inhibitor UNC10245092
UNC10245131 has improved permeability and stability relative to UNC10245092.
improved permeability and stability over previously identified linear peptide inhibitor UNC10245092
UNC10245131 has improved permeability and stability relative to UNC10245092.
improved permeability and stability over previously identified linear peptide inhibitor UNC10245092
UNC10245131 has improved permeability and stability relative to UNC10245092.
improved permeability and stability over previously identified linear peptide inhibitor UNC10245092
UNC10245131 has improved permeability and stability relative to UNC10245092.
improved permeability and stability over previously identified linear peptide inhibitor UNC10245092
UNC10245131 lacks cytotoxicity relative to UNC10245092.
Unlike UNC10245092, UNC10245131 lacks cytotoxicity
UNC10245131 lacks cytotoxicity relative to UNC10245092.
Unlike UNC10245092, UNC10245131 lacks cytotoxicity
UNC10245131 lacks cytotoxicity relative to UNC10245092.
Unlike UNC10245092, UNC10245131 lacks cytotoxicity
UNC10245131 lacks cytotoxicity relative to UNC10245092.
Unlike UNC10245092, UNC10245131 lacks cytotoxicity
UNC10245131 lacks cytotoxicity relative to UNC10245092.
Unlike UNC10245092, UNC10245131 lacks cytotoxicity
UNC10245131 lacks cytotoxicity relative to UNC10245092.
Unlike UNC10245092, UNC10245131 lacks cytotoxicity
UNC10245131 lacks cytotoxicity relative to UNC10245092.
Unlike UNC10245092, UNC10245131 lacks cytotoxicity
mRNA display was used to discover new cyclic peptide inhibitors of CIB1.
we deploy mRNA display to discover new cyclic peptide inhibitors
mRNA display was used to discover new cyclic peptide inhibitors of CIB1.
we deploy mRNA display to discover new cyclic peptide inhibitors
mRNA display was used to discover new cyclic peptide inhibitors of CIB1.
we deploy mRNA display to discover new cyclic peptide inhibitors
mRNA display was used to discover new cyclic peptide inhibitors of CIB1.
we deploy mRNA display to discover new cyclic peptide inhibitors
mRNA display was used to discover new cyclic peptide inhibitors of CIB1.
we deploy mRNA display to discover new cyclic peptide inhibitors
mRNA display was used to discover new cyclic peptide inhibitors of CIB1.
we deploy mRNA display to discover new cyclic peptide inhibitors
mRNA display was used to discover new cyclic peptide inhibitors of CIB1.
we deploy mRNA display to discover new cyclic peptide inhibitors
UNC10245131 does not affect downstream signaling, unlike UNC10245092.
Unlike UNC10245092, UNC10245131 lacks cytotoxicity and does not affect downstream signaling.
UNC10245131 does not affect downstream signaling, unlike UNC10245092.
Unlike UNC10245092, UNC10245131 lacks cytotoxicity and does not affect downstream signaling.
UNC10245131 does not affect downstream signaling, unlike UNC10245092.
Unlike UNC10245092, UNC10245131 lacks cytotoxicity and does not affect downstream signaling.
UNC10245131 does not affect downstream signaling, unlike UNC10245092.
Unlike UNC10245092, UNC10245131 lacks cytotoxicity and does not affect downstream signaling.
UNC10245131 does not affect downstream signaling, unlike UNC10245092.
Unlike UNC10245092, UNC10245131 lacks cytotoxicity and does not affect downstream signaling.
UNC10245131 does not affect downstream signaling, unlike UNC10245092.
Unlike UNC10245092, UNC10245131 lacks cytotoxicity and does not affect downstream signaling.
UNC10245131 does not affect downstream signaling, unlike UNC10245092.
Unlike UNC10245092, UNC10245131 lacks cytotoxicity and does not affect downstream signaling.
UNC10245131 is a potent ligand for CIB1 that could help clarify CIB1 biological roles.
UNC10245131 is a potent ligand that could aid in clarifying roles of CIB1 in TNBC survival and proliferation and other CIB1-associated biological phenotypes.
UNC10245131 is a potent ligand for CIB1 that could help clarify CIB1 biological roles.
UNC10245131 is a potent ligand that could aid in clarifying roles of CIB1 in TNBC survival and proliferation and other CIB1-associated biological phenotypes.
UNC10245131 is a potent ligand for CIB1 that could help clarify CIB1 biological roles.
UNC10245131 is a potent ligand that could aid in clarifying roles of CIB1 in TNBC survival and proliferation and other CIB1-associated biological phenotypes.
UNC10245131 is a potent ligand for CIB1 that could help clarify CIB1 biological roles.
UNC10245131 is a potent ligand that could aid in clarifying roles of CIB1 in TNBC survival and proliferation and other CIB1-associated biological phenotypes.
UNC10245131 is a potent ligand for CIB1 that could help clarify CIB1 biological roles.
UNC10245131 is a potent ligand that could aid in clarifying roles of CIB1 in TNBC survival and proliferation and other CIB1-associated biological phenotypes.
UNC10245131 is a potent ligand for CIB1 that could help clarify CIB1 biological roles.
UNC10245131 is a potent ligand that could aid in clarifying roles of CIB1 in TNBC survival and proliferation and other CIB1-associated biological phenotypes.
UNC10245131 is a potent ligand for CIB1 that could help clarify CIB1 biological roles.
UNC10245131 is a potent ligand that could aid in clarifying roles of CIB1 in TNBC survival and proliferation and other CIB1-associated biological phenotypes.
UNC10245131 shows good selectivity for CIB1 over other EF-hand domain proteins.
good selectivity for CIB1 over other EF-hand domain proteins
UNC10245131 shows good selectivity for CIB1 over other EF-hand domain proteins.
good selectivity for CIB1 over other EF-hand domain proteins
UNC10245131 shows good selectivity for CIB1 over other EF-hand domain proteins.
good selectivity for CIB1 over other EF-hand domain proteins
UNC10245131 shows good selectivity for CIB1 over other EF-hand domain proteins.
good selectivity for CIB1 over other EF-hand domain proteins
UNC10245131 shows good selectivity for CIB1 over other EF-hand domain proteins.
good selectivity for CIB1 over other EF-hand domain proteins
UNC10245131 shows good selectivity for CIB1 over other EF-hand domain proteins.
good selectivity for CIB1 over other EF-hand domain proteins
UNC10245131 shows good selectivity for CIB1 over other EF-hand domain proteins.
good selectivity for CIB1 over other EF-hand domain proteins
UNC10245092 binds CIB1 with low nanomolar affinity.
Both assays showed that the peptide bound to CIB1 with low nanomolar affinity.
binding affinity low nanomolar
UNC10245092 binds CIB1 with low nanomolar affinity.
Both assays showed that the peptide bound to CIB1 with low nanomolar affinity.
binding affinity low nanomolar
UNC10245092 binds CIB1 with low nanomolar affinity.
Both assays showed that the peptide bound to CIB1 with low nanomolar affinity.
binding affinity low nanomolar
UNC10245092 binds CIB1 with low nanomolar affinity.
Both assays showed that the peptide bound to CIB1 with low nanomolar affinity.
binding affinity low nanomolar
UNC10245092 binds CIB1 with low nanomolar affinity.
Both assays showed that the peptide bound to CIB1 with low nanomolar affinity.
binding affinity low nanomolar
UNC10245092 binds CIB1 with low nanomolar affinity.
Both assays showed that the peptide bound to CIB1 with low nanomolar affinity.
binding affinity low nanomolar
UNC10245092 binds CIB1 with low nanomolar affinity.
Both assays showed that the peptide bound to CIB1 with low nanomolar affinity.
binding affinity low nanomolar
Tat-derived CPP-derivatized UNC10245092 shows effects on TNBC cells in culture that are consistent with CIB1 depletion.
UNC10245092 was further derivatized with a C-terminal Tat-derived cell penetrating peptide (CPP) to demonstrate its effects on TNBC cells in culture, which are consistent with results of CIB1 depletion.
Tat-derived CPP-derivatized UNC10245092 shows effects on TNBC cells in culture that are consistent with CIB1 depletion.
UNC10245092 was further derivatized with a C-terminal Tat-derived cell penetrating peptide (CPP) to demonstrate its effects on TNBC cells in culture, which are consistent with results of CIB1 depletion.
Tat-derived CPP-derivatized UNC10245092 shows effects on TNBC cells in culture that are consistent with CIB1 depletion.
UNC10245092 was further derivatized with a C-terminal Tat-derived cell penetrating peptide (CPP) to demonstrate its effects on TNBC cells in culture, which are consistent with results of CIB1 depletion.
Tat-derived CPP-derivatized UNC10245092 shows effects on TNBC cells in culture that are consistent with CIB1 depletion.
UNC10245092 was further derivatized with a C-terminal Tat-derived cell penetrating peptide (CPP) to demonstrate its effects on TNBC cells in culture, which are consistent with results of CIB1 depletion.
Tat-derived CPP-derivatized UNC10245092 shows effects on TNBC cells in culture that are consistent with CIB1 depletion.
UNC10245092 was further derivatized with a C-terminal Tat-derived cell penetrating peptide (CPP) to demonstrate its effects on TNBC cells in culture, which are consistent with results of CIB1 depletion.
Tat-derived CPP-derivatized UNC10245092 shows effects on TNBC cells in culture that are consistent with CIB1 depletion.
UNC10245092 was further derivatized with a C-terminal Tat-derived cell penetrating peptide (CPP) to demonstrate its effects on TNBC cells in culture, which are consistent with results of CIB1 depletion.
Tat-derived CPP-derivatized UNC10245092 shows effects on TNBC cells in culture that are consistent with CIB1 depletion.
UNC10245092 was further derivatized with a C-terminal Tat-derived cell penetrating peptide (CPP) to demonstrate its effects on TNBC cells in culture, which are consistent with results of CIB1 depletion.
UNC10245092 binds as an alpha-helix in the CIB1 H10 pocket and displaces the CIB1 C-terminal H10 helix, causing conformational changes in H7 and H8.
the 2.1 Å resolution structure revealed that the peptide binds as an α-helix in the H10 pocket, displacing the CIB1 C-terminal H10 helix and causing conformational changes in H7 and H8
structure resolution 2.1 Å
UNC10245092 binds as an alpha-helix in the CIB1 H10 pocket and displaces the CIB1 C-terminal H10 helix, causing conformational changes in H7 and H8.
the 2.1 Å resolution structure revealed that the peptide binds as an α-helix in the H10 pocket, displacing the CIB1 C-terminal H10 helix and causing conformational changes in H7 and H8
structure resolution 2.1 Å
UNC10245092 binds as an alpha-helix in the CIB1 H10 pocket and displaces the CIB1 C-terminal H10 helix, causing conformational changes in H7 and H8.
the 2.1 Å resolution structure revealed that the peptide binds as an α-helix in the H10 pocket, displacing the CIB1 C-terminal H10 helix and causing conformational changes in H7 and H8
structure resolution 2.1 Å
UNC10245092 binds as an alpha-helix in the CIB1 H10 pocket and displaces the CIB1 C-terminal H10 helix, causing conformational changes in H7 and H8.
the 2.1 Å resolution structure revealed that the peptide binds as an α-helix in the H10 pocket, displacing the CIB1 C-terminal H10 helix and causing conformational changes in H7 and H8
structure resolution 2.1 Å
UNC10245092 binds as an alpha-helix in the CIB1 H10 pocket and displaces the CIB1 C-terminal H10 helix, causing conformational changes in H7 and H8.
the 2.1 Å resolution structure revealed that the peptide binds as an α-helix in the H10 pocket, displacing the CIB1 C-terminal H10 helix and causing conformational changes in H7 and H8
structure resolution 2.1 Å
UNC10245092 binds as an alpha-helix in the CIB1 H10 pocket and displaces the CIB1 C-terminal H10 helix, causing conformational changes in H7 and H8.
the 2.1 Å resolution structure revealed that the peptide binds as an α-helix in the H10 pocket, displacing the CIB1 C-terminal H10 helix and causing conformational changes in H7 and H8
structure resolution 2.1 Å
UNC10245092 binds as an alpha-helix in the CIB1 H10 pocket and displaces the CIB1 C-terminal H10 helix, causing conformational changes in H7 and H8.
the 2.1 Å resolution structure revealed that the peptide binds as an α-helix in the H10 pocket, displacing the CIB1 C-terminal H10 helix and causing conformational changes in H7 and H8
structure resolution 2.1 Å
The studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
These studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
The studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
These studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
The studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
These studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
The studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
These studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
The studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
These studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
The studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
These studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
The studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
These studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
Approval Evidence
4 sources10 linked approval claimsfirst-pass slug unc10245092
reference peptide (UNC10245092)
Source:
The crystal structure CIB1 in complex with peptide inhibitor UNC10245092 was retrieved from the protein databank.
Source:
previously identified linear peptide inhibitor UNC10245092
Source:
The top peptide sequence selected, UNC10245092
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:
comparative bindingsupports
Among the top five selected designed peptides, mutant 2 showed stronger interactions with CIB1 than the reference peptide UNC10245092.
Our results indicate that amongst the top five selected peptides, mutant 2 nd mutant have strong interactions with CIB1 than the reference peptide (UNC10245092)
Source:
design goalsupports
The study aimed to design novel peptides from the reference peptide UNC10245092 to target CIB1 using residue scan methodology.
The goal of this study is to design novel peptides from the reference peptide (UNC10245092) through residue scan methodology.
Source:
comparative propertysupports
UNC10245131 has improved permeability and stability relative to UNC10245092.
improved permeability and stability over previously identified linear peptide inhibitor UNC10245092
Source:
cytotoxicitysupports
UNC10245131 lacks cytotoxicity relative to UNC10245092.
Unlike UNC10245092, UNC10245131 lacks cytotoxicity
Source:
downstream signaling effectsupports
UNC10245131 does not affect downstream signaling, unlike UNC10245092.
Unlike UNC10245092, UNC10245131 lacks cytotoxicity and does not affect downstream signaling.
Source:
bindingsupports
UNC10245092 binds CIB1 with low nanomolar affinity.
Both assays showed that the peptide bound to CIB1 with low nanomolar affinity.
Source:
structural mechanismsupports
UNC10245092 binds as an alpha-helix in the CIB1 H10 pocket and displaces the CIB1 C-terminal H10 helix, causing conformational changes in H7 and H8.
the 2.1 Å resolution structure revealed that the peptide binds as an α-helix in the H10 pocket, displacing the CIB1 C-terminal H10 helix and causing conformational changes in H7 and H8
Source:
tool classificationsupports
The studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
These studies provide a first-in-class chemical tool for CIB1 inhibition in cell culture and validate the CIB1 H10 pocket for future probe and drug discovery efforts.
Source:
Comparisons
Source-backed strengths
A key strength is that UNC10245092 is a previously identified CIB1-binding linear peptide inhibitor with structural characterization in complex with its target. It also served as the comparator in later computational studies, where designed mutant peptides were evaluated against it for CIB1 interaction and predicted inhibitory potential.
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)
Source:
Our results indicate that amongst the top five selected peptides, mutant 2 nd mutant have strong interactions with CIB1 than the reference peptide (UNC10245092)
Source:
improved permeability and stability over previously identified linear peptide inhibitor UNC10245092
Compared with FLIPs
UNC10245092 and FLIPs address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: conformational_uncaging
Strengths here: appears more independently replicated; looks easier to implement in practice.
Compared with Product Nkabinde
UNC10245092 and Product Nkabinde address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; same primary input modality: chemical
Strengths here: appears more independently replicated; looks easier to implement in practice.
Compared with ProKAS module
UNC10245092 and ProKAS module address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; same primary input modality: chemical
Strengths here: appears more independently replicated; looks easier to implement in practice.
Ranked Citations
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