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Results for "

antibiotic residue

" in MedChemExpress (MCE) Product Catalog:

By Targets:	Antibiotic (15) Bacterial (13) CRM1 (1) Dengue Virus (1) Flavivirus (1) Fungal (2) Herbicide (1) HIV (1) Parasite (1)
By Research Areas:	Cancer (3) Infection (18) Inflammation/Immunology (1) Metabolic Disease (1)

Inhibitors & Agonists

Screening Libraries

Peptides

Natural
Products

Targets Recommended: Antibiotic

Cat. No.	Product Name	Target	Research Areas	Chemical Structure

HY-P0274A

PGLa TFA	Bacterial Antibiotic	Infection
PGLa TFA, a 21-residue peptide, is an antimicrobial peptide. PGLa TFA is a member of the magainin family of antibiotic peptides found in frog skin and its secretions .

HY-117430

Hymeglusin F-244; 1233A; L-659699	Flavivirus Dengue Virus Antibiotic	Infection Metabolic Disease Cancer
Hymeglusin, as a fungal β-lactone *antibiotic, is a HMG-CoA* synthase inhibitor (IC₅₀ = 0.12 μM). Hymeglusin covalently modifies the active Cys ¹²⁹ residue of the enzyme .

HY-16909

Leptomycin B Maximum Cited Publications 9 Publications Verification CI 940; LMB	CRM1 Fungal Antibiotic	Infection Cancer
Leptomycin B (CI 940; LMB) is a potent inhibitor of the nuclear export of proteins. Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue. Leptomycin B is a potent antifungal antibiotic blocking the eukaryotic cell cycle .

HY-P0274

PGLa	Bacterial Antibiotic	Infection
PGLa, a 21-residue peptide, is an antimicrobial peptide. PGLa is a member of the magainin family of antibiotic peptides found in frog skin and its secretions .

HY-139798

Iboxamycin	Bacterial	Infection
Iboxamycin is a potent *antibiotic* candidate bearing a fused bicyclic amino acid residue. Iboxamycin is orally bioavailable, safe and effective in researching both Gram-positive and Gram-negative bacterial infections in mice .

HY-P10857

Microcin J25 MccJ25	Bacterial Antibiotic	Infection
Microcin J25 (MccJ25) is a cyclic peptide antibiotic consisting of 21 unmodified amino acid residues. Microcin J25 inhibits DNA-dependent RNA polymerase (RNAP) of Gram-negative bacteria. Microcin J25 has antibacterial activity .

HY-136821

Polymyxin D2	Bacterial Antibiotic	Infection
Polymyxin D2 is an antibiotic discovered from Bacillus polymyxa, exhibiting antibacterial activity. Its core structure consists of a cyclic heptapeptide moiety and a tripeptide side chain with a fatty acyl residue. Polymyxin D2 can be used in anti-infective research .

HY-125104

Mirosamicin	Antibiotic Bacterial	Infection
Mirosamicin is an antibiotic with high antibacterial activity that targets a wide range of gram-positive bacteria and certain Gram-negative bacteria as well as mycoplasma. Mirosamicin can be used for research in the field of food safety monitoring .

HY-118043

RK-1441B	Antibiotic	Infection
RK-1441B is an anti-phage antibiotic produced by Streptomyces sp. RK-1441 and belongs to the pyrrolo[1,4]benzodiazepine class. RK-1441B has antiphage activity but no significant antimicrobial activity against a supersusceptible E. coli strain to an antitumor antibiotic. RK-1441B is inactive in vitro and may be converted to the active form in the host organism. Its fellow antibiotic RK-1441A can form an adduct with guanine residues in the DNA chain to exert resistance .

HY-129252

Prothracarcin	Antibiotic Bacterial	Infection Cancer
Prothracarcin is an antibiotic with antitumor activity that exerts its tumor cell toxicity by covalently binding to the C-2 amino group of guanine residues in the minor groove of DNA. Prothracarcin also shows antibacterial activity against Gram-positive bacteria and some Gram-negative bacteria such as Escherichia coli .

HY-106783

Polymyxin B nonapeptide 2 Publications Verification	Bacterial Antibiotic	Infection
Polymyxin B nonapeptide is a cyclic peptide obtained from Polymyxin B by proteolytic removal of its terminal amino acyl residue. Polymyxin B nonapeptide is less toxic, lacks bactericidal activity, and retains its ability to render gram-negative bacteria susceptible to several antibiotics by permeabilizing their outer membranes .

HY-106783A

Polymyxin B nonapeptide TFA 2 Publications Verification	Bacterial Antibiotic	Infection
Polymyxin B nonapeptide TFA is a cyclic peptide obtained from Polymyxin B by proteolytic removal of its terminal amino acyl residue. Polymyxin B nonapeptide TFA is less toxic, lacks bactericidal activity, and retains its ability to render gram-negative bacteria susceptible to several antibiotics by permeabilizing their outer membranes .

HY-106783R

Polymyxin B nonapeptide (Standard)	Bacterial Antibiotic	Infection
Polymyxin B nonapeptide (Standard) is the analytical standard of Polymyxin B nonapeptide. This product is intended for research and analytical applications. Polymyxin B nonapeptide is a cyclic peptide obtained from Polymyxin B by proteolytic removal of its terminal amino acyl residue. Polymyxin B nonapeptide is less toxic, lacks bactericidal activity, and retains its ability to render gram-negative bacteria susceptible to several antibiotics by permeabilizing their outer membranes[1][2][3].

HY-P10795

NK-2 antibiotic NK 2	Parasite Bacterial Fungal	Infection
NK-2 (Antibiotic NK 2), a shortened linear amphipathic NK-Lysin analog (comprising residues 39 to 65 of NK-lysin), is an antimicrobial peptide that exhibits potent activities against trypanosoma cruzi, Candida albicans, gram-positive and gram-negative bacteria. NK-2 can kill trypanosomes residing inside the human glioblastoma cell line 86HG39, left the host cells apparently unharmed .

HY-P2200

Siamycin I BMY-29304	HIV Antibiotic	Infection Inflammation/Immunology
Siamycin I (BMY-29304), a 21-residue tricyclic peptide, is a secondary metabolite in actinomycetes. Siamycin I is a HIV fusion inhibitor with ED₅₀s of 0.05 to 5.7 μM for acute HIV type 1 (HIV-1) and HIV-2 infections. Siamycin I inhibits the gelatinase and gelatinase biosynthesis-activating pheromone (GBAP) signaling via the FsrC-FsrA two-component regulatory system in a noncompetitive manner. Siamycin I suppresses the expression of both fsrBDC and gelE-sprE transcripts. Siamycin I, a lasso peptide, interacts with lipid II and inhibits cell wall biosynthesis. Siamycin I, an antibiotic, has the potential for enterococcal infections research .

HY-106783AR

Polymyxin B nonapeptide TFA (Standard)	Bacterial Antibiotic	Infection
Polymyxin B nonapeptide (TFA) (Standard) is the analytical standard of Polymyxin B nonapeptide (TFA). This product is intended for research and analytical applications. Polymyxin B nonapeptide TFA is a cyclic peptide obtained from Polymyxin B by proteolytic removal of its terminal amino acyl residue. Polymyxin B nonapeptide TFA is less toxic, lacks bactericidal activity, and retains its ability to render gram-negative bacteria susceptible to several antibiotics by permeabilizing their outer membranes[1][2][3].

HY-115894

DapL-IN-1	Herbicide	Infection
DapL-IN-1 is an inhibitor of L,L-diaminoheptanoic acid aminotransferase (DapL) with the characteristics of inhibiting DapL activity in bacteria and plants. DapL-IN-1 can be used to design and discover new biocides such as antibiotics, herbicides or algaecides with the potential to be non-toxic to animals. DapL-IN-1 shows differential sensitivity in inhibiting different DapL homologues, which can provide important information for further drug development. DapL-IN-1 may affect its biological activity by affecting the interaction with residues adjacent to the active site, which may lead to different binding modes .

HY-P5712

Gramicidin S 1 Publications Verification Gramicidin soviet	Antibiotic Bacterial	Infection
Gramicidin S 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 .

Cat. No.	Product Name

HY-L042

Glycoside Compound Library	809 compounds
Glycosides are compounds in which a sugar group is bonded through its anomeric carbon to another group via a glycosidic bond. Many biologically active compounds are glycosides. Glycosides comprise several important classes of compounds such as hormones, sweeteners, alkaloids, flavonoids, antibiotics, etc. The glycosidic residue can be crucial for their activity or can only improve pharmacokinetic parameters. Glycosides, which exhibit anti-inflammatory, anti-infection, anti-cancer and anti-oxidative properties, play numerous important roles in living organisms, such as streptomycin, as an aminoglycoside antibiotic, has anti-infection activity. Anthracyclines possess good antibacterial and anti-cancer activities. MCE Glycoside Compound Library contains a unique collection of 809 glycoside compounds and is a useful tool to discovery glycoside drugs.

Glycoside Compound Library

809 compounds

Glycosides are compounds in which a sugar group is bonded through its anomeric carbon to another group via a glycosidic bond. Many biologically active compounds are glycosides. Glycosides comprise several important classes of compounds such as hormones, sweeteners, alkaloids, flavonoids, antibiotics, etc. The glycosidic residue can be crucial for their activity or can only improve pharmacokinetic parameters. Glycosides, which exhibit anti-inflammatory, anti-infection, anti-cancer and anti-oxidative properties, play numerous important roles in living organisms, such as streptomycin, as an aminoglycoside antibiotic, has anti-infection activity. Anthracyclines possess good antibacterial and anti-cancer activities.

MCE Glycoside Compound Library contains a unique collection of 809 glycoside compounds and is a useful tool to discovery glycoside drugs.

HY-L914

Serine/Threonine Focused Covalent Fragment Library	3,300 compounds
In the research of covalent inhibitors targeting serine and threonine, scientists have found that the nucleophilicity of these hydroxyl groups is significantly enhanced due to the influence of their surrounding environment. This results in higher activity during catalytic reactions. Aspirin, which targets the non-catalytic domain serine (Ser529 in human COX1) of cyclooxygenase, exerts its anti-inflammatory effect through covalent binding. β-lactam antibiotics, which targets the catalytic domain serine of penicillin-binding proteins, interferes with bacterial cell wall synthesis. 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 3,300 fragment molecules which can target serine and threonine residues and can be used for fragment-based covalent drug discovery.

Serine/Threonine Focused Covalent Fragment Library

3,300 compounds

In the research of covalent inhibitors targeting serine and threonine, scientists have found that the nucleophilicity of these hydroxyl groups is significantly enhanced due to the influence of their surrounding environment. This results in higher activity during catalytic reactions. Aspirin, which targets the non-catalytic domain serine (Ser529 in human COX1) of cyclooxygenase, exerts its anti-inflammatory effect through covalent binding. β-lactam antibiotics, which targets the catalytic domain serine of penicillin-binding proteins, interferes with bacterial cell wall synthesis.

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 3,300 fragment molecules which can target serine and threonine residues and can be used for fragment-based covalent drug discovery.

Cat. No.	Product Name	Target	Research Area