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Results for "

competition binding

" in MedChemExpress (MCE) Product Catalog:

By Targets:	iGluR (1) Insulin Receptor (2)
By Research Areas:	Inflammation/Immunology (1) Metabolic Disease (2) Neurological Disease (1)

Inhibitors & Agonists

Screening Libraries

Peptides

Targets Recommended: Penicillin-binding protein (PBP) FKBP FABP Transthyretin (TTR) Ligands for Target Protein for PROTAC YB-1 GHR P-glycoprotein

Cat. No.	Product Name	Target	Research Areas	Chemical Structure

HY-109520

Glatiramer acetate	Others	Inflammation/Immunology
Glatiramer acetate, a synthetic analogue of myelin basic protein and an immunomodulating agent, can be used for the research of multiple sclerosis. Glatiramer acetate exhibits strong and promiscuous binding to MHC molecules and consequent competition with various myelin antigens for their presentation to T cells. A further aspect of its action is potent induction of specific suppressor cells of the T helper 2 (Th2) type that migrate to the brain and lead to in situ bystander suppression .

HY-P10138

human GIP(3-30), amide	Insulin Receptor	Metabolic Disease
human GIP(3-30), amide is a high affinity antagonist of the human GIP receptor in vitro .

HY-P10138A

human GIP(3-30), amide TFA	Insulin Receptor	Metabolic Disease
human GIP(3-30), amide TFA is a high affinity antagonist of the human GIP receptor in vitro .

HY-118424

JNJ-55511118	iGluR	Neurological Disease
JNJ-55511118 is a highly potent, reversible, and selective AMPA receptor inhibitor selective for TARP-γ8. JNJ-55511118 fully displaces the radioligand (20 nM) with the K_i of 26 nM in competition binding experiments. JNJ-55511118 is a tool molecule with potential therapeutic utility as an anticonvulsant or neuroprotectant .

HY-118124

2-Iodoestradiol	Others	Others
2-Iodoestradiol is a potent human sex hormone binding globulin (SHBG) ligand with a remarkably high affinity for SHBG. 2-Iodoestradiol exhibits competition for the same binding site as dihydrotestosterone in binding to human SHBG. The binding affinity constant of 2-Iodoestradiol at physiological pH and 37 degrees Celsius is 2.4 x 10(9) M-1, exceeding that for SHBG. 2-Iodoestradiol has been shown to bind to serum albumin, but with lower affinity. The radioisotope 125I-derivative of 2-Iodoestradiol has been used to study the binding properties of human SHBG, demonstrating its potential application in biological research .

Cat. No.	Product Name

HY-L907

MCE Kinase Hinge Binder Fragment Library	10,000 compounds
The most prominent mechanism of action of kinase inhibitors is their competition with ATP by binding to the hinge region of the kinase protein. Once the kinase is blocked by an inhibitor, it loses the ability to transfer phosphate groups from ATP to other molecules, resulting in the loss of kinase activity. The hinge-binding region of kinase inhibitors mimics the interaction pattern between the ATP nucleobase and the kinase. MCE extracted thousands of kinase inhibitors from the ChEMBL database and isolated their molecular fragments. In certain cases, the amino and amide groups on the molecular fragments are crucial for binding in the hinge region. Therefore, we enhanced the diversity of the collected results by adding these two groups to unoccupied positions on the ring system. Subsequently, the fragments were assessed for their hinge region binding ability via docking at distinct kinases, we also applied pharmacophore constraints to ensure interactions with key amino acids in the kinase hinge region, ultimately obtaining kinase-related molecular fragments. MCE provides over 10,000 kinase fragment molecules that meet the above requirements and are available off the shelf, serving as an effective tool for screening and developing drugs targeting kinases.

MCE Kinase Hinge Binder Fragment Library

10,000 compounds

The most prominent mechanism of action of kinase inhibitors is their competition with ATP by binding to the hinge region of the kinase protein. Once the kinase is blocked by an inhibitor, it loses the ability to transfer phosphate groups from ATP to other molecules, resulting in the loss of kinase activity.

The hinge-binding region of kinase inhibitors mimics the interaction pattern between the ATP nucleobase and the kinase. MCE extracted thousands of kinase inhibitors from the ChEMBL database and isolated their molecular fragments. In certain cases, the amino and amide groups on the molecular fragments are crucial for binding in the hinge region. Therefore, we enhanced the diversity of the collected results by adding these two groups to unoccupied positions on the ring system. Subsequently, the fragments were assessed for their hinge region binding ability via docking at distinct kinases, we also applied pharmacophore constraints to ensure interactions with key amino acids in the kinase hinge region, ultimately obtaining kinase-related molecular fragments.

MCE provides over 10,000 kinase fragment molecules that meet the above requirements and are available off the shelf, serving as an effective tool for screening and developing drugs targeting kinases.

human GIP(3-30), amide	Insulin Receptor	Metabolic Disease
human GIP(3-30), amide is a high affinity antagonist of the human GIP receptor in vitro .

human GIP(3-30), amide TFA	Insulin Receptor	Metabolic Disease
human GIP(3-30), amide TFA is a high affinity antagonist of the human GIP receptor in vitro .

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