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Results for "

hydrophobic amino acid

" in MedChemExpress (MCE) Product Catalog:

By Targets:	Acyltransferase (1) Adrenergic Receptor (1) Antibiotic (1) Bacterial (2) Biochemical Assay Reagents (2) Drug Intermediate (1) Endogenous Metabolite (10) Glycosidase (1) Isotope-Labeled Compounds (6) Liposome (4) Na+/K+ ATPase (1) nAChR (2) Pyruvate Kinase (1) SARS-CoV (1) Virus Protease (1)
By Research Areas:	Cardiovascular Disease (3) Infection (3) Metabolic Disease (3) Neurological Disease (2)
Oligonucleotides:	Cationic Lipids (4)

Inhibitors & Agonists

Screening Libraries

Biochemical Assay Reagents

Peptides

Natural
Products

Isotope-Labeled Compounds

Oligonucleotides

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

Cat. No.	상품명	Target	연구분야	Chemical Structure

HY-N0771S2

L-Isoleucine-15N	Isotope-Labeled Compounds Endogenous Metabolite	Others
L-Isoleucine-15N is the 15N-labeled L-Isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid. L-Isoleucine is an essential amino acid .

HY-N0771S

L-Isoleucine-13C6	Isotope-Labeled Compounds Endogenous Metabolite	Others
L-Isoleucine- ¹³C₆ is the ¹³C-labeled L-Isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid . L-Isoleucine is an essential amino acid.

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-B0952

2-Aminoheptane 1 Publications Verification Tuaminoheptane	Adrenergic Receptor	Neurological Disease
2-Aminoheptane (Tuaminoheptane) is a norepinephrine transporter inhibitor. 2-Aminoheptane binds to norepinephrine transporter via ionic and hydrophobic interactions to block norepinephrine uptake. 2-Aminoheptane deactivates ω-TAmla enzyme, reduces recombinant whole cell stability, and acts as an amino group donor substrate for ω-TA and ω-TAmla enzymes. 2-Aminoheptane can be used in research on depression and Alzheimer's disease .

HY-N0771S9

L-Isoleucine-13C6,15N	Isotope-Labeled Compounds	Others
L-Isoleucine- ¹³C₆, ¹⁵N is ¹³C and ¹⁵N labeled L-isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid . L-Isoleucine is an essential amino acid.

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-N0771S1

DL-Isoleucine-d10	Isotope-Labeled Compounds Endogenous Metabolite	Others
DL-Isoleucine-d₁₀ is the deuterium labeled L-Isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid . L-Isoleucine is an essential amino acid.

HY-N0771S4

L-Isoleucine-1-13C 1 Publications Verification	Endogenous Metabolite	Others
L-Isoleucine-1- ¹³C is the ¹³C-labeled L-Isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid . L-Isoleucine is an essential amino acid.

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-W142092

N-Acetyl-DL-serine	Bacterial Endogenous Metabolite	Others
N-Acetyl-DL-serine is a hydrophobic amino acid that is synthesized in the body and can be found as a free form or as a salt with malonate, phosphate, or acetate. N-Acetyl-DL-serine has antimicrobial activity against Bacillus cereus and Staphylococcus aureus. N-Acetyl-DL-serine has also been used for the immobilization of DNA fragments on solid surfaces and can be used for protein synthesis and optical detection of DNA strands .

HY-N0771S3

L-Isoleucine-d10 1 Publications Verification	Endogenous Metabolite	Others
L-Isoleucine-d₁₀ is the deuterium labeled L-Isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid . L-Isoleucine is an essential amino acid.

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-Y0425

Terephthalaldehyde	Drug Intermediate Biochemical Assay Reagents	Others
Terephthalaldehyde is a crosslinking agent. Terephthalaldehyde forms a crosslinked structure inside the gelatin matrix by forming Schiff base imines with the amino groups of gelatin, thereby constructing a three-dimensional network. Terephthalaldehyde improves the hydrophobicity of the gelatin matrix, delays water vapor penetration and enhances the liquid water resistance of gelatin films. Terephthalaldehyde can be used as a crosslinking agent to prepare crosslinked chitosan hydrogel (CAAT) via ultrasound-induced synthesis. Terephthalaldehyde helps CAAT hydrogels selectively adsorb anionic dyes from aqueous media, including multi-component systems containing cationic dyes. Terephthalaldehyde serves as a starting material for the synthesis of bis-heterocyclic compounds (including bis-thiazole and bis-triazolopyrimidine compounds) .

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-N0771S5

L-Isoleucine-13C6,15N,d10	Endogenous Metabolite	Others
L-Isoleucine- ¹³C₆, ¹⁵N,d₁₀ is the deuterium, ¹³C-, and 15-labeled L-Isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid . L-Isoleucine is an essential amino acid.

HY-N0771S8

L-Isoleucine-d1	Isotope-Labeled Compounds Endogenous Metabolite	Others
L-Isoleucine-d is the deuterium labeled L-Isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid . L-Isoleucine is an essential amino acid.

HY-N0771S7

L-Isoleucine-15N,d10	Endogenous Metabolite	Others
L-Isoleucine- ¹⁵N,d₁₀ is the deuterium and ¹⁵N-labeled L-Isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid[1]. L-Isoleucine is an essential amino acid.

HY-N0771S6

L-Cysteine-13C3,15N,d3 Cysteine-¹³C₃,¹⁵N,d₃	Isotope-Labeled Compounds Endogenous Metabolite	Others
L-Cysteine- ¹³C₃, ¹⁵N,d₃ is the deuterium, ¹³C-, and 15-labeled L-Isoleucine (HY-Y0337). L-isoleucine is a nonpolar hydrophobic amino acid . L-Isoleucine is an essential amino acid.

HY-W440681

C13-112-tri-tail	Liposome	Others
C13-112-tri-tail is a cationic lipid-like compound containing a polar amino alcohol head group, three hydrophobic carbon-13 tails, and a PEG2 linker. C13-112-tri-tail can be formulated into a lipid nanoparticle (LNP).

HY-W440684

C13-113-tetra-tail	Liposome	Others
C13-113-tetra tail is a cationic lipid-like compound containing a polar amino alcohol head group, four hydrophobic carbon-13 tails, and a tertiary amine linker. C13-113-tetra tail can be formulated into a lipid nanoparticle (LNP).

HY-W440683

C13-112-tetra-tail	Liposome	Others
C13-112-tetra-tail is a cationic lipid-like compound containing a polar amino alcohol head group, four hydrophobic carbon-13 tails, and a PEG2 linker. C13-112-tetra-tail can be formulated into a lipid nanoparticle (LNP).

HY-W440682

C13-113-tri-tail	Liposome	Others
C13-113-tri tail is a cationic lipid-like compound containing a polar amino alcohol head group, three hydrophobic carbon-13 tails, and a tertiary amine linker. C13-113-tri tail can be formulated into a lipid nanoparticle (LNP).

HY-149341

α-Glucosidase-IN-28	Glycosidase	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-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-P1748A

Thermolysin, Geobacillus stearothermophilus	Biochemical Assay Reagents	Metabolic Disease
Thermolysin (Geobacillus stearothermophilus (EC 3.4.24.27)) is a thermostable neutral metalloproteinase. It requires one zinc ion to maintain enzyme activity and four calcium ions to maintain structural stability. Thermolysin (Geobacillus stearothermophilus (EC 3.4.24.27) specifically catalyzes the hydrolysis of peptide bonds containing hydrophobic amino acids.

HY-182613

NSC-2888		Cardiovascular Disease
NSC-2888 is a Rho kinase II (ROCK-II) inhibitor with an IC₅₀ of 8.4 nM against human targets. NSC-2888 inhibits enzymatic activity by binding to active site amino acids via hydrogen bonds and hydrophobic interactions. NSC-2888 induces relaxation of pre-contracted rat aortic strips. NSC-2888 can be used in research related to hypertension .

Cat. No.	상품명

HY-L928

GPCR Targeted Diversity Library	7,116 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 7,116 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

7,116 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 7,116 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.

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.

Cat. No.	상품명	Type

HY-Y0425

Terephthalaldehyde	Biochemical Assay Reagents
Terephthalaldehyde is a crosslinking agent. Terephthalaldehyde forms a crosslinked structure inside the gelatin matrix by forming Schiff base imines with the amino groups of gelatin, thereby constructing a three-dimensional network. Terephthalaldehyde improves the hydrophobicity of the gelatin matrix, delays water vapor penetration and enhances the liquid water resistance of gelatin films. Terephthalaldehyde can be used as a crosslinking agent to prepare crosslinked chitosan hydrogel (CAAT) via ultrasound-induced synthesis. Terephthalaldehyde helps CAAT hydrogels selectively adsorb anionic dyes from aqueous media, including multi-component systems containing cationic dyes. Terephthalaldehyde serves as a starting material for the synthesis of bis-heterocyclic compounds (including bis-thiazole and bis-triazolopyrimidine compounds) .

Terephthalaldehyde

Biochemical Assay Reagents

Terephthalaldehyde is a crosslinking agent. Terephthalaldehyde forms a crosslinked structure inside the gelatin matrix by forming Schiff base imines with the amino groups of gelatin, thereby constructing a three-dimensional network. Terephthalaldehyde improves the hydrophobicity of the gelatin matrix, delays water vapor penetration and enhances the liquid water resistance of gelatin films. Terephthalaldehyde can be used as a crosslinking agent to prepare crosslinked chitosan hydrogel (CAAT) via ultrasound-induced synthesis. Terephthalaldehyde helps CAAT hydrogels selectively adsorb anionic dyes from aqueous media, including multi-component systems containing cationic dyes. Terephthalaldehyde serves as a starting material for the synthesis of bis-heterocyclic compounds (including bis-thiazole and bis-triazolopyrimidine compounds) .

HY-W440681

C13-112-tri-tail	Biochemical Assay Reagents
C13-112-tri-tail is a cationic lipid-like compound containing a polar amino alcohol head group, three hydrophobic carbon-13 tails, and a PEG2 linker. C13-112-tri-tail can be formulated into a lipid nanoparticle (LNP).

HY-W440684

C13-113-tetra-tail	Biochemical Assay Reagents
C13-113-tetra tail is a cationic lipid-like compound containing a polar amino alcohol head group, four hydrophobic carbon-13 tails, and a tertiary amine linker. C13-113-tetra tail can be formulated into a lipid nanoparticle (LNP).

HY-W440683

C13-112-tetra-tail	Biochemical Assay Reagents
C13-112-tetra-tail is a cationic lipid-like compound containing a polar amino alcohol head group, four hydrophobic carbon-13 tails, and a PEG2 linker. C13-112-tetra-tail can be formulated into a lipid nanoparticle (LNP).

HY-W440682

C13-113-tri-tail	Biochemical Assay Reagents
C13-113-tri tail is a cationic lipid-like compound containing a polar amino alcohol head group, three hydrophobic carbon-13 tails, and a tertiary amine linker. C13-113-tri tail can be formulated into a lipid nanoparticle (LNP).

Cat. No.	상품명	Target	Research Area

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-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-W142092

N-Acetyl-DL-serine	Bacterial Endogenous Metabolite	Others
N-Acetyl-DL-serine is a hydrophobic amino acid that is synthesized in the body and can be found as a free form or as a salt with malonate, phosphate, or acetate. N-Acetyl-DL-serine has antimicrobial activity against Bacillus cereus and Staphylococcus aureus. N-Acetyl-DL-serine has also been used for the immobilization of DNA fragments on solid surfaces and can be used for protein synthesis and optical detection of DNA strands .

HY-P5429

DNA-PK Substrate	Peptides	Others
DNA-PK Substrate is a biological active peptide. (A substrate for DNA-dependent protein kinase (DNA-PK), phosphorylation. DNA-PK is essential for the repair of DNA double-strand breaks. This peptide corresponding to 11–24 amino acids of human p53 with threonine 18 and serine 20 changed to alanine is used as a substrate for the assay of DNA-PK activityPyroglutamyl (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-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-P4371A

Hel 13-5 TFA	Peptides	Others
Hel 13-5 TFA is a monomeric synthetic peptide based on the N-terminal fragment of human SP-B. Hel 13-5 TFA is mainly α-helical and consists of 13 hydrophobic amino acid residues and 5 hydrophilic amino acid residues. Hel 13-5 TFA can be combined with phospholipids for the development of a model system for pulmonary surfactant .

HY-P5479

EE epitope	Peptides	Others
EE epitope is a biological active peptide. (This peptide is a 314 to 319 amino acids fragment of the middle T antigen of mouse polymavirus. Glu-Glu epitope peptide is widely used as an epitope tag.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.)

Cat. No.	상품명	Category	Target	Chemical Structure

HY-N15451

Deoxytopsentin	Structural Classification Alkaloids Marine natural products Sponge Indole Alkaloids Source Classification	Pyruvate Kinase
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-N15365

Antcin B	Structural Classification Microorganisms Ketones, Aldehydes, Acids Source Classification	Virus Protease SARS-CoV
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 .

Cat. No.	상품명	Chemical Structure

HY-N0771S2

L-Isoleucine-15N
L-Isoleucine-15N is the 15N-labeled L-Isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid. L-Isoleucine is an essential amino acid .

HY-N0771S

L-Isoleucine-13C6
L-Isoleucine- ¹³C₆ is the ¹³C-labeled L-Isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid . L-Isoleucine is an essential amino acid.

HY-N0771S9

L-Isoleucine-13C6,15N
L-Isoleucine- ¹³C₆, ¹⁵N is ¹³C and ¹⁵N labeled L-isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid . L-Isoleucine is an essential amino acid.

HY-N0771S1

DL-Isoleucine-d10
DL-Isoleucine-d₁₀ is the deuterium labeled L-Isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid . L-Isoleucine is an essential amino acid.

HY-N0771S4

L-Isoleucine-1-13C 1 Publications Verification
L-Isoleucine-1- ¹³C is the ¹³C-labeled L-Isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid . L-Isoleucine is an essential amino acid.

HY-N0771S3

L-Isoleucine-d10 1 Publications Verification
L-Isoleucine-d₁₀ is the deuterium labeled L-Isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid . L-Isoleucine is an essential amino acid.

HY-N0771S5

L-Isoleucine-13C6,15N,d10
L-Isoleucine- ¹³C₆, ¹⁵N,d₁₀ is the deuterium, ¹³C-, and 15-labeled L-Isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid . L-Isoleucine is an essential amino acid.

HY-N0771S8

L-Isoleucine-d1
L-Isoleucine-d is the deuterium labeled L-Isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid . L-Isoleucine is an essential amino acid.

HY-N0771S7

L-Isoleucine-15N,d10
L-Isoleucine- ¹⁵N,d₁₀ is the deuterium and ¹⁵N-labeled L-Isoleucine. L-isoleucine is a nonpolar hydrophobic amino acid[1]. L-Isoleucine is an essential amino acid.

HY-N0771S6

L-Cysteine-13C3,15N,d3
L-Cysteine- ¹³C₃, ¹⁵N,d₃ is the deuterium, ¹³C-, and 15-labeled L-Isoleucine (HY-Y0337). L-isoleucine is a nonpolar hydrophobic amino acid . L-Isoleucine is an essential amino acid.

Cat. No.	상품명		Classification

HY-W440681

C13-112-tri-tail		Cationic Lipids
C13-112-tri-tail is a cationic lipid-like compound containing a polar amino alcohol head group, three hydrophobic carbon-13 tails, and a PEG2 linker. C13-112-tri-tail can be formulated into a lipid nanoparticle (LNP).

HY-W440684

C13-113-tetra-tail		Cationic Lipids
C13-113-tetra tail is a cationic lipid-like compound containing a polar amino alcohol head group, four hydrophobic carbon-13 tails, and a tertiary amine linker. C13-113-tetra tail can be formulated into a lipid nanoparticle (LNP).

HY-W440683

C13-112-tetra-tail		Cationic Lipids
C13-112-tetra-tail is a cationic lipid-like compound containing a polar amino alcohol head group, four hydrophobic carbon-13 tails, and a PEG2 linker. C13-112-tetra-tail can be formulated into a lipid nanoparticle (LNP).

HY-W440682

C13-113-tri-tail		Cationic Lipids
C13-113-tri tail is a cationic lipid-like compound containing a polar amino alcohol head group, three hydrophobic carbon-13 tails, and a tertiary amine linker. C13-113-tri tail can be formulated into a lipid nanoparticle (LNP).

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hydrophobic amino acid

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Peptides

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