Search Result

Results for "

hydrophobic amino acid residues

" in MedChemExpress (MCE) Product Catalog:

By Targets:	Acyltransferase (1) Antibiotic (1) Bacterial (1) Biochemical Assay Reagents (1) Endogenous Metabolite (1) Na+/K+ ATPase (1) nAChR (2) Pyruvate Kinase (1) SARS-CoV (1) Virus Protease (1)
By Research Areas:	Cardiovascular Disease (2) Infection (3) Metabolic Disease (1) Neurological Disease (1)

Inhibitors & Agonists

Screening Libraries

Peptides

Natural
Products

Targets Recommended: Amino Acid Decarboxylase Amino Acid Oxidase Amino Acid Derivatives Amino acid Transporter Branched Chain Amino Acid Transaminase (BCAT) EAAT

Cat. No.	Product Name	Target	Research Areas	Chemical Structure

HY-P5712

Gramicidin S 1 Publications Verification Gramicidin soviet	Antibiotic Bacterial Na+/K+ ATPase	Infection
Gramicidin S (Gramicidin soviet) is a cationic cyclic peptide antibiotic that selectively targets bacterial cell membranes and has anticancer activity. Gramicidin S also exerts antibacterial activity by destroying membrane integrity and interfering with membrane protein function. Gramicidin S inserts into the phospholipid bilayer through hydrophobic amino acid residues, specifically binds to negatively charged membrane lipids and disrupts membrane structure, thereby inhibiting cell division and cell wall synthesis, and ultimately causing bacterial death. Gramicidin S also inhibits ion channels, with IC₅₀s of 41 μM, 24 μM, and 3 μM for Na ⁺/K ⁺-ATPase, tobacco leaf plasma membrane Mg ²⁺/K ⁺-ATPase, and rat heart plasma membrane Ca ²⁺-ATPase, respectively .

HY-157521

AANAT-IN-1	Acyltransferase	Neurological Disease Metabolic Disease
AANAT-IN-1 is an arylalkylamine N-acetyltransferase (AANAT) inhibitor with a sheep AANAT IC₅₀ of 9.9 μM. AANAT-IN-1 binds to the active site of sheep AANAT, interacting with amino acid residues via hydrogen bonds, hydrophobic interactions, ionic interactions, and water bridges, inhibiting the enzyme's catalytic activity. AANAT-IN-1 can be used for the researches of circadian rhythm-associated neuropsychiatric conditions, seasonal affective disorder, and other diseases associated with abnormally elevated melatonin levels .

HY-P1271

Catestatin Catestatin (cattle)	nAChR	Cardiovascular Disease
Catestatin is a 21-amino acid residue, cationic and hydrophobic peptide. Catestatin is an endogenous peptide that regulates cardiac function and blood pressure . Catestatin is a non-competitive nicotinic antagonist acting through nicotinic acetylcholine receptors (nAChRs) to inhibit catecholamine release .

HY-N15451

Deoxytopsentin	Pyruvate Kinase	Infection
Deoxytopsentin (compound 5) is a marine bisindole alkaloid and also a MRSA pyruvate kinase inhibitor. Deoxytopsentin exists in sponges. Deoxytopsentin exhibits antibacterial activity against methicillin-resistant Staphylococcus aureus strains in vitro .

HY-P1271A

Catestatin TFA	nAChR	Cardiovascular Disease
Catestatin TFA is a 21-amino acid residue, cationic and hydrophobic peptide. Catestatin TFA is an endogenous peptide that regulates cardiac function and blood pressure . Catestatin TFA is a non-competitive nicotinic antagonist acting through nicotinic acetylcholine receptors (nAChRs) to inhibit catecholamine release .

HY-N15365

Antcin B	Virus Protease SARS-CoV	Infection
Antcin B is a SARS-CoV-2 3-chymotrypsin-like protease (3CL Pro) inhibitor. Antcin B binds to multiple key amino acid residues of 3CL Pro(such as Leu141, Asn142, Glu166, His163, etc.) through hydrogen bonds, salt bridges, and hydrophobic interactions, thereby inhibiting the activity of 3CL Pro, blocking the cleavage process of viral polyproteins, and suppressing the replication of the SARS-CoV-2 virus in host cells. Antcin B is promising for research of COVID-19 .

HY-E71364

Pepsin (USP)	Endogenous Metabolite	Others
Pepsin (USP) is a proteolytic enzyme. Pepsin (USP) catalyzes cleavage of peptide bonds in proteins and synthetic peptides. Pepsin (USP) dissolves protein nutrients, cleaves proteins into peptones, produces large polypeptides, smaller peptides, and free amino acids, affects amino acid release rates and protein allergenicity. Pepsin (USP) can be used for biochemical research .

HY-P11905

FcIII peptide	Biochemical Assay Reagents	Others
FcIII peptide is a 13-amino-acid peptide that competitively binds the hinge region of IgG Fc fragment with high affinity. FcIII peptide has an inhibition constant K_i of 25 nM when competing with Protein A for binding sites. FcIII peptide displays high selectivity toward human IgG subtypes yet weak binding affinity for murine IgG1. FcIII peptide anchors IgG Fc through hydrophobic interactions formed by tryptophan and valine residues, alongside multiple hydrogen bonds and salt bridges. FcIII peptide alters the local microenvironment of conjugated fluorescein after binding IgG Fc, which triggers enhanced fluorescent signals. FcIII peptide can be applied to researches related to monoclonal antibody production. .

Cat. No.	Product Name

HY-L913

Tyrosine Focused Covalent Fragment Library	104 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

104 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.

HY-L928

GPCR Targeted Diversity Library	7,121 compounds
G protein-coupled receptors (GPCRs) are membrane proteins in humans and one of the most important targets in drug discovery. Approximately 35% of launched drugs are targeted GPCRs, making them a crucial class of targets in drug discovery. The orthosteric site of a GPCR is its endogenous ligand’s (such as neurotransmitters or hormones) binding site. This site plays a central role in signal transduction. Small molecules binding to this site typically contain a protonatable amino group, enabling the formation of salt bridges or hydrogen bonds with acidic residues in the binding pocket. In contrast, the allosteric site does not directly initiate signaling but modulates the signal intensity of the GPCR by altering or stabilizing the conformation of the orthosteric site. Small molecules binding to the allosteric site often contain multiple aromatic rings to occupy hydrophobic pockets and achieve their functional effects. MCE has collected over 7,121 reported bioactive molecules targeting GPCRs, covering Class A, B, and C GPCRs. These small molecules were subjected to AI representation to extract 2D and 3D features. Subsequently, we do screening by AI score based on similarity to identify molecules in diversity library highly similar to the reported bioactive molecules in both 2D and 3D, with a threshold greater than 0.7. Further screening based on cLogP was applied to select molecules with good lipophilicity, which facilitates the binding of small molecules to GPCRs. This diversity library can be widely applied to the discovery of compounds targeting GPCR proteins.

GPCR Targeted Diversity Library

7,121 compounds

G protein-coupled receptors (GPCRs) are membrane proteins in humans and one of the most important targets in drug discovery. Approximately 35% of launched drugs are targeted GPCRs, making them a crucial class of targets in drug discovery.

The orthosteric site of a GPCR is its endogenous ligand’s (such as neurotransmitters or hormones) binding site. This site plays a central role in signal transduction. Small molecules binding to this site typically contain a protonatable amino group, enabling the formation of salt bridges or hydrogen bonds with acidic residues in the binding pocket. In contrast, the allosteric site does not directly initiate signaling but modulates the signal intensity of the GPCR by altering or stabilizing the conformation of the orthosteric site. Small molecules binding to the allosteric site often contain multiple aromatic rings to occupy hydrophobic pockets and achieve their functional effects.

MCE has collected over 7,121 reported bioactive molecules targeting GPCRs, covering Class A, B, and C GPCRs. These small molecules were subjected to AI representation to extract 2D and 3D features. Subsequently, we do screening by AI score based on similarity to identify molecules in diversity library highly similar to the reported bioactive molecules in both 2D and 3D, with a threshold greater than 0.7. Further screening based on cLogP was applied to select molecules with good lipophilicity, which facilitates the binding of small molecules to GPCRs. This diversity library can be widely applied to the discovery of compounds targeting GPCR proteins.

Cat. No.	Product Name	Target	Research Area