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Results for "

Hydrophobic interaction

" in MedChemExpress (MCE) Product Catalog:

By Targets:	Aldehyde Dehydrogenase (ALDH) (2) Antibiotic (2) Autophagy (1) Bcr-Abl (1) Beta-secretase (2) Biochemical Assay Reagents (1) CCR (1) CDK (1) DNA Stain (3) DNA/RNA Synthesis (1) Eukaryotic Initiation Factor (eIF) (1) Fat Mass and Obesity-associated Protein (FTO) (1) Glucosidase (3) HIV (1) MARCKS (1) Parasite (3) PKC (1) Polo-like Kinase (PLK) (1) Ras (1) TMV (1) Tyrosinase (1)
By Research Areas:	Cancer (6) Endocrinology (1) Infection (8) Inflammation/Immunology (1) Metabolic Disease (4) Neurological Disease (2)

Inhibitors & Agonists

Screening Libraries

Biochemical Assay Reagents

Peptides

Natural
Products

Isotope-Labeled Compounds

Cat. No.	Product Name	Target	Research Areas	Chemical Structure

HY-B1953

Thiacloprid	Parasite DNA Stain	Infection
Thiacloprid, a chloronicotinyl insecticide, is targeted chiefly to control aphid pest species in orchards and vegetables . Thiacloprid destabilizes DNA. Thiacloprid changes the structure and stability of DNA through binding into the minor groove by hydrophobic or hydrogen interactions .

HY-139031

ALDH1A2-IN-1	Aldehyde Dehydrogenase (ALDH)	Endocrinology
ALDH1A2-IN-1 is an active site-directed reversible ALDH1A2 inhibitor (IC₅₀=0.91 μM; Kd=0.26 μM) with several hydrophobic interactions .

HY-164645

pan-KRAS-IN-16	Ras	Cancer
pan-KRAS-IN-16 is an anti-RAS small molecule derived from an intracellular antibody fragment with pan-RAS-effector protein-protein interaction inhibitor properties. pan-KRAS-IN-16 binds to a hydrophobic pocket near to the effector-binding switch regions of RAS. pan-KRAS-IN-16 prevents endogenous RAS-dependent signaling in tumor cell lines .

HY-157245

Hydrophobic polishing resin	Others	Others
Hydrophobic polishing resin is an agarose filler that can be used in hydrophobic interaction chromatography (The average particle size: 40 μm) .

HY-157244

Proteins separation resin	Others	Others
Proteins separation resin is a hydrophobic interaction chromatography resin that can be used in the monoclonal antibody purification (Particle size: 65 μm) .

HY-147879

α-Glucosidase-IN-8	Glucosidase	Metabolic Disease
α-Glucosidase-IN-8 (Compound 4k) is a competitive α-glucosidase inhibitor with an IC₅₀ of 0.18 µg/mL .

HY-139032

CM121	Aldehyde Dehydrogenase (ALDH)	Others
CM121 is an active site-directed reversible ALDH1A2 inhibitor (IC₅₀=0.54 μM；Kd=1.1 μM) with a variety of hydrophobic interactions .

HY-163201

TMV-IN-7	TMV	Infection
TMV-IN-7 (compound G2) is a potent inhibitor of tobacco mosaic virus (TMV). TMV-IN-7 exhibits strong hydrophobic interactions to obstructing the virus’s self-assembly .

HY-B1953S

Thiacloprid-d4	DNA Stain Parasite	Infection
Thiacloprid-d₄ is the deuterium labeled Thiacloprid[1]. Thiacloprid, a chloronicotinyl insecticide, is targeted chiefly to control aphid pest species in orchards and vegetables[1]. Thiacloprid destabilizes DNA. Thiacloprid changes the structure and stability of DNA through binding into the minor groove by hydrophobic or hydrogen interactions[2].

HY-W154333

H-Arg-OtBu dihydrochloride	Antibiotic	Infection
H-Arg-OtBu (dihydrochloride) is a membrane-targeting antimicrobial. H-Arg-OtBu (dihydrochloride) targets the negatively charged bacterial membrane via a combination of electrostatic and hydrophobic interactions. H-Arg-OtBu (dihydrochloride) can be used for bacterial infections diseases research .

HY-W105775

Diammonium succinate Ammonium succinate	Biochemical Assay Reagents	Others
Diammonium succinate (Ammonium succinate) is a hydrophobic hydrocarbon compound that can be used to study its interaction with microbial cells, especially the mechanisms of degradation and bioavailability. Diammonium succinate is a biomaterial or organic compound that can be used as a biomaterial or organic compound related to life science research.

HY-B1953R

Thiacloprid (Standard)	Parasite DNA Stain	Infection
Thiacloprid (Standard) is the analytical standard of Thiacloprid. This product is intended for research and analytical applications. Thiacloprid, a chloronicotinyl insecticide, is targeted chiefly to control aphid pest species in orchards and vegetables . Thiacloprid destabilizes DNA. Thiacloprid changes the structure and stability of DNA through binding into the minor groove by hydrophobic or hydrogen interactions .

HY-N2204

Swertiajaponin	Tyrosinase	Inflammation/Immunology
Swertiajaponin is a tyrosinase inhibitor, forms multiple hydrogen bonds and hydrophobic interactions with the binding pocket of tyrosinase, with an IC₅₀ of 43.47 μM. Swertiajaponin also inhibits oxidative stress-mediated MAPK/MITF signaling, leading to decrease in tyrosinase protein level. Swertiajaponin suppresses melanin accumulation and exhibits strong anti-oxidative activity .

HY-162512

CB-0821	CCR HIV	Infection
CB-0821 is a high affinity CCR5 inhibitor with a K_i of 0.04 nM. CB-0821 binds efficiently to the hydrophobic pocket of the CCR5 protein, to inhibit the interactions between viral protein and CCR5, thereby inhibiting viral entry. CB-0821 has the potential for anti-HIV research .

HY-160478

GNF-6	Bcr-Abl	Cancer
GNF-6 (Compound 14) inhibits the gatekeeper threonine residue mutation of BCR-ABL-T315I with IC₅₀s of 0.25 μM, 0.09 μM and 0.590 μM for c-ABL-T334I, BCR-ABL and BCR-ABL-T315I variants, respectively. GNF-6, an ATP competitive inhibitor, disrupts the assembly of the hydrophobic spine (a network of hydrophobic interactions), thereby locking the kinase in an inactive ‘DFG-out’ conformation .

HY-120465

ZINC36617540	Others	Infection
ZINC36617540 is a novel Nef protein inhibitor with anti-HIV activity. ZINC36617540 exhibits superior binding affinity by binding to Nef protein. ZINC36617540 shows a similar binding mode to the prototype molecule B9 in molecular docking. The mechanism of action of ZINC36617540 mainly depends on its hydrophobic and electrostatic interactions with Nef protein .

HY-129265

Poloxin-2	Polo-like Kinase (PLK)	Cancer
Poloxin-2 is a small molecule Plk1 PBD inhibitor that can effectively induce cell mitotic arrest with an EC50 of approximately 15 μM in HeLa cells. Poloxin-2HT was developed by conjugating a hydrophobic tag (HT) to Poloxin-2, a new application of inhibitors targeting protein-protein interactions. Poloxin-2HT significantly enhanced the effects on cell viability and apoptosis by selectively degrading Plk1 protein, and its effect was stronger than that of untagged Poloxin-2. These data validate hydrophobic tags as a new strategy for targeting and disrupting disease-associated proteins.

HY-156405

FTO-IN-10	Fat Mass and Obesity-associated Protein (FTO) Autophagy	Metabolic Disease
FTO-IN-10 (compound 7) is a potent human demethylase FTO (the fat mass and obesity-associated protein) inhibitor with an IC₅₀ of 4.5 μM. FTO-IN-10 enters the FTO’s structural domain II binding pocket through hydrophobic and hydrogen bonding interactions. FTO-IN-10 induces DNA damage and autophagic cell death in A549 cells .

HY-16035A

Alatrofloxacin mesylate	DNA/RNA Synthesis Others Antibiotic	Infection
Alatrofloxacin mesylate is an antibiotic with antibacterial activity. Alatrofloxacin mesylate exhibits significant hydrophilicity in the aqueous phase, forming a very stable suspension. The degradation products of Alatrofloxacin mesylate become hydrophobic upon exposure, causing aggregation of its particles. The long-term stability of Alatrofloxacin mesylate is closely related to its polar interaction. The changes in surface tension characteristics of Alatrofloxacin mesylate particles under different lighting conditions affect their physical and chemical properties .

HY-149341

α-Glucosidase-IN-28	Glucosidase	Metabolic Disease
α-Glucosidase-IN-28 (Compound 18) is a α-Glucosidase inhibitor (IC₅₀: 0.62 μM, K_i: 3.93 μM). α-Glucosidase-IN-28 binds to α-glucosidase at the original binding site (OBS), and forms multiple hydrophobic interactions with nearby amino acids. α-Glucosidase-IN-28 can be used for research of diabetes and related diseases .

HY-156078

α-Glucosidase-IN-32	Glucosidase	Metabolic Disease
α-Glucosidase-IN-32 (compound f26) is a reversible, noncompetitive and orally active α-glucosidase inhibitor with an IC₅₀ value of 3.07 μM. α-Glucosidase-IN-32 complex with α-glucosidase through hydrogen bonds and hydrophobic interactions, led to changes in the conformation and secondary strictures of α-glucosidase and further the inhibition of the enzymatic activity. α-Glucosidase-IN-32 can be used for diabetic disease research .

HY-120646

BMS-242	Others	Others
BMS-242 is a small molecule PD-1/PD-L1 inhibitor with the activity of inhibiting the PD-1/PD-L1 interaction. BMS-242 can bind to the hydrophobic channel pocket between PD-L1 molecules, inhibit the PD-1/PD-L1 immune checkpoint pathway, and provide a new way for cancer inhibition.

HY-123045

PNU-292137	CDK	Cancer
PNU-292137 is an orally active, potent CDK2 inhibitor with IC₅₀s of 37 nM and 92 nM for CDK2/cyclin A and CDK2/cyclin E, respectively. PNU-292137 makes interactions with the hydrophobic pocket at the back of the CDK2 ATP pocket. PNU-292137 efficiently inhibits tumor cell proliferation in human colon and prostate tumor cell lines. PNU-292137 exhibits antitumor activity (TGI>50%) in a mouse xenograft model .

HY-144739

BACE1-IN-8	Beta-secretase	Neurological Disease
BACE1-IN-8 (compound 70b) is a potent BACE1 (β-site APP cleaving enzyme 1) inhibitor, with an IC₅₀ of 3.9 µM .

HY-144741

BACE1-IN-9	Beta-secretase	Neurological Disease
BACE1-IN-9 (compound 82b) is a potent BACE1 (β-site APP cleaving enzyme 1) inhibitor, with an IC₅₀ of 1.2 µM .

HY-19831A

(Z)-4EGI-1	Eukaryotic Initiation Factor (eIF)	Cancer
(Z)-4EGI-1 is the Z-isomer of 4EGI-1 and is an inhibitor of eIF4E/eIF4G interaction and of translation initiation. (Z)-4EGI-1 effectively binds to eIF4E with an IC₅₀ of 43.5 μM and a K_d value of 8.74 μM. (Z)-4EGI-1 has anticancer activity .

HY-P5439

Epsilon-V1-2, Cys-conjugated	PKC MARCKS	Others
Epsilon-V1-2, Cys-conjugated is a biological active peptide. (This peptide is the εPKC specific inhibitor. Its inhibitory activity is based on εPKC translocation and MARCKS phosphorylation. This peptide interferes with εPKC interaction with the anchoring protein εRACK. This peptide contains a cysteine residue added to the C-terminus for potential S-S bond formation with a carrier protein.Pyroglutamyl (pGlu) peptides may spontaneously form when either Glutamine (Q) or Glutamic acid (E) is located at the sequence N-terminus. The conversion of Q or E to pGlu is a natural occurrence and in general it is believed that the hydrophobic γ-lactam ring of pGlu may play a role in peptide stability against gastrointestinal proteases. Pyroglutamyl peptides are therefore considered a normal subset of such peptides and are included as part of the peptide purity during HPLC analysis.)

HY-121690

Semotiadil SD-3211	Others	Others
Semotiadil is a novel calcium antagonist whose stereochemical structure was investigated by X-ray crystallography and circular dichroism spectroscopy. X-ray structural analysis was performed using its enantiomeric salts with (S)-(+)-mandelic acid (2); 1 (mandelate salt). The R absolute configuration of 1, which was previously determined by chemical transformation of an optically active synthetic precursor, was directly confirmed by this analysis. Hydrogen bonding, charge repulsion, and hydrophobic interactions that stabilize the crystal structure were observed in the crystals. Circular dichroism spectra of 1 (mandelate salt) and 1 (hydrofuranate salt) in ethanolic solution showed similar spectral patterns. The CD bands of each chromophore were unambiguously assigned, and the conformation of the benzothiazole ring was determined using the optical rotation rule. The X-ray and CD data confirmed the P conformation of the benzothiazole ring and the equatorial position of the 2-phenyl ring in both the crystal and ethanolic solution states. These findings are in good agreement with our previous results on the conformational analysis of 2-arylbenzothiazole derivatives.

HY-118097

GW0072	Others	Cancer
Targeted molecular dynamics simulations of the entry of GW0072, a macromolecular ligand with flexible ionic properties, into the ligand-binding domain of the nuclear receptor PPARc were performed. Starting from the apo-form, where the ligand is located outside the receptor, the simulation ultimately locks the ligand into the binding pocket, yielding a structure very close to the holo-form. The results show that the entry process is mainly guided by hydrophobic interactions, and that the entry and exit pathways are very similar. We suggest that the TMD approach may be useful in distinguishing ligands generated by in silico docking. To address the question of the ligand entry process, we report targeted molecular dynamics (TMD) simulations of the binding of the GW0072 ligand to the ligand-binding domain (LBD) of the peroxisome proliferator-activated receptor gamma (PPARc). PPARc is a member of the nuclear receptor superfamily and an important agent target for many diseases. We chose to study this complex because (i) GW0072 is a large ionic, highly flexible ligand that includes aliphatic chains and polar groups, and (ii) previous simulations have defined a possible escape pathway for this ligand. Starting from the apo-form of the receptor (PDB.ID 1PRG, chain A), with the ligand located outside, TMD simulations converged on a holo-form complex that is close to the target structure (PDB.ID 4PRG, chain A), defining a permeation pathway into the binding pocket that is very similar to the escape pathway. However, during the entry of GW0072 into the receptor (Fig. 5), the helices are very mobile, and once the ligand is placed in the pocket, AF-2 becomes more rigid during the remainder of the simulation (Fig. S1 in the Supplementary Materials). This finding is in good agreement with the observations of Oberfield et al. [12], suggesting that despite the absence of direct interaction with the ligand, the presence of the ligand in the binding site stabilizes an intermediate conformation of AF-2, which may be responsible for the property of GW0072 as a partial agonist.

Cat. No.	Product Name

HY-L913

Tyrosine Focused Covalent Fragment Library	124 compounds
Recently, significant advancements in tyrosine-targeting electrophiles have primarily occurred in the field of protein-protein interactions (PPIs), where cysteine residues are often underrepresented and novel chemistries are needed to address these interfaces. In this context, tyrosines are frequently more accessible compared to more buried binding sites. Moreover, they are commonly found at "hot spots," which are functional epitopes of PPIs, with 12.3% of the residues consisting of tyrosines. This prevalence is likely due to the hydrophobic nature of tyrosine, its ability to participate in aromatic π-interactions, and its capacity for hydrogen bonding. Beyond PPIs, some progress has also been made in covalent tyrosine targeting in other areas where more commonly addressed side chains are lacking. Even though tyrosine has a slightly lower pKa value compared to the protonated lysine side chain (approximately 10 vs. 10.5 for the unprotected amino acid side chains), significantly less progress has been made in the development of tyrosine-targeted covalent ligands compared to lysine. This is likely due to the reduced flexibility of the tyrosine side chain and the greater steric hindrance of its hydroxy group, which makes it more challenging to adopt suitable reaction geometries. Through careful selection, we constructed a structural filter containing over 110 electrophilic groups. By analyzing the electrophilic fragments selected by the structural filter, we removed any molecules with trivial or undesirable structural features. Ultimately, we obtained 124 fragment molecules which can target tyrosine residue and can be used for fragment-based covalent drug discovery.

Tyrosine Focused Covalent Fragment Library

124 compounds

Recently, significant advancements in tyrosine-targeting electrophiles have primarily occurred in the field of protein-protein interactions (PPIs), where cysteine residues are often underrepresented and novel chemistries are needed to address these interfaces. In this context, tyrosines are frequently more accessible compared to more buried binding sites. Moreover, they are commonly found at "hot spots," which are functional epitopes of PPIs, with 12.3% of the residues consisting of tyrosines. This prevalence is likely due to the hydrophobic nature of tyrosine, its ability to participate in aromatic π-interactions, and its capacity for hydrogen bonding. Beyond PPIs, some progress has also been made in covalent tyrosine targeting in other areas where more commonly addressed side chains are lacking. Even though tyrosine has a slightly lower pKa value compared to the protonated lysine side chain (approximately 10 vs. 10.5 for the unprotected amino acid side chains), significantly less progress has been made in the development of tyrosine-targeted covalent ligands compared to lysine. This is likely due to the reduced flexibility of the tyrosine side chain and the greater steric hindrance of its hydroxy group, which makes it more challenging to adopt suitable reaction geometries.

Through careful selection, we constructed a structural filter containing over 110 electrophilic groups. By analyzing the electrophilic fragments selected by the structural filter, we removed any molecules with trivial or undesirable structural features. Ultimately, we obtained 124 fragment molecules which can target tyrosine residue and can be used for fragment-based covalent drug discovery.

Cat. No.	Product Name	Type