GlycoAntibiotic Array

10612

From: $864.00

The GlycoAntibiotic array allows researchers to explore the interactions between glycopeptide antibiotics and biological samples such as proteins, antibodies, cells, cell lysate, serum, vesicles, bacteria, or viral particles. The Multivalent Surface Coating (MSC) technology allows efficient immobilization of carbohydrate-based antibiotic molecules on a solid microarray surface for high-throughput binding analysis. This array features 23 glycopeptide antibiotics. Each array slide contains 8 or 16 identical subarrays, enabling the simultaneous analysis of various samples. The glycopeptide antibiotic array can be customized to meet individual client needs. Assay services are available upon request.

SKU: 10612 Category:
Description
Structures
Examples
Document

Description

Combating bacterial infection has been an ongoing medical challenge since early civilization. Historical examples include Yersinia pestis, the bacterium responsible for the Black Plague, and Vibrio cholera, the bacterium causing cholera. However, as modern medicine evolves, microbes also evolve. Antibiotic resistance becomes a growing public health concern as microbes acquire drug-resistant genes driven by the overuse or misuse of antibiotics. For example, strains of bacteria such as methicillin-resistant Staphylococcus aureus (MRSA) are increasingly prevalent in clinical settings, putting patients with weakened immune systems at risk. The number of deaths due to antibiotic-resistant diseases is predicted to reach 10 million annual deaths by 2050, surpassing the cancer mortality rate. A sharp decline in the development and approval of new antibiotics further exacerbates the challenge of drug resistance.

Common antibiotic mechanisms of action include the selective inhibition of RNA translation by the bacterial ribosome, as well as inhibiting the biosynthesis of the bacterial cell wall. Because of their ability to bind to the ribosome, several carbohydrate-based antibiotics are also considered candidates for cancer, genetic disorders, HIV, and AIDS treatments. Carbohydrate-based antibiotics and their derivatives present a promising avenue for antimicrobial agent development. However, the efficacy of these compounds is affected by binding to plasma proteins and antibiotic-targeting enzymes produced by the bacterium. A promising strategy to overcome this limitation is to chemically modify the structure of existing, naturally derived antibiotics to circumvent undesirable bindings. Therefore, uncovering the binding partners to evaluate the strength of compound interaction is critical for developing efficient antibiotic agents.

ZBiotech has developed a robust microarray platform that allows researchers to explore the interactions between glycopeptide antibiotics and biological samples such as proteins, antibodies, cells, cell lysate, serum, vesicles, bacteria, or viral particles. The Multivalent Surface Coating (MSC) technology allows efficient immobilization of carbohydrate-based antibiotic molecules on a solid microarray surface for high-throughput binding analysis. This array features 23 glycopeptide antibiotics. Each array slide contains 8 or 16 identical subarrays, enabling the simultaneous analysis of various samples. The glycopeptide antibiotic array can be customized to meet individual client needs. Assay services are available upon request.

Features

  • 23 glycopeptide antibiotics;
  • Unrivaled sensitivity and specificity;
  • Simple assay format;
  • Small sample volume;
  • Customizable (select glycopeptide antibiotics for a specific microarray format)
  • Assay service available;

Applications

  • Evaluate binding specificities of antibiotic-interacting proteins or antibodies;
  • Evaluate binding specificities of antibiotic-interacting bacteria;

Structures

List of structures of glycopeptide antibiotics on the array (download the PDF)

Antibiotic Array ID Structure Name
Amikacin GA-1 O-3-Amino-3-deoxy-a-D-glucopyranosyl-(1→6)-O-[6-amino-6-deoxy-a-D-glucopyranosyl-(1→4)]-N1-(4-amino-2-hydroxy-1-oxobutyl)-2-deoxy-D-streptamine
Kanamycin B GA-2 O-3-Amino-3-deoxy-a-D-glucopyranosyl-(1→4)-O-(2,6-diamino-2,6-dideoxy-a-D-glucopyranosyl-(1→6))-2-deoxy-D-Streptamine
Tobramycin GA-3 O-3-Amino-3-deoxy-a-D-glucopyranosyl-(1→6)-O-[2,6-diamino-2,3,6-trideoxy-a-D-ribo-hexopyranosyl(1→4)]-2-deoxy-D-streptamine
Dibekacin GA-4 O-3-Amino-3-deoxy-a-D-glucopyranosyl-(1→6)-O-[2,6-diamino-2,3,4,6-tetradeoxy-a-D-erythro-hexopyranosyl-(1→4)]-2-deoxy-D-streptamine
Gentamycin GA-5 4,6-diamino-3-{[3-deoxy-4-c-methyl-3-(methylamino)pentopyranosyl]oxy}-2-hydroxycyclohexyl 2-amino-2,3,4,6,7-pentadeoxy-6-(methylamino)heptopyranoside
Sisomicin GA-6 O-3-deoxy-4-C-methyl-3-(methylamino)-β-L-arabinopyranosyl-(1→6)-O-(2,6-diamino-2,3,4,6-tetradeoxy-α-D-glycero-hex-4-enopyranosyl-(1→4))-2-deoxy-D-Streptamine
Netilmicin GA-7 O-3-deoxy-4-C-methyl-3-(methylamino)-β-L-arabinopyranosyl-(1→6)-O-[2,6-diamino-2,3,4,6-tetradeoxy-α-D-glycero-hex-4-enopyranosyl-(1→4)]-2-deoxy-N1-ethyl-D-Streptamine
Neomycin GA-8 O-2,6-diamino-2,6-dideoxy-α-D-glucopyranosyl-(1→4)-O-(O-2,6-diamino-2,6-dideoxy-β-L-idopyranosyl-(1-3)-β-D-ribofuranosyl-(1→5))-2-deoxy-D-Streptamine
Paromomycin GA-9 O-2,6-Diamino-2,6-dideoxy-b-L-idopyranosyl-(1→3)-O-b-D-ribofuranosyl-(1®5)-O-[2-amino-2-deoxy-a-D-glucopyranosyl-(1→4)]-2-deoxystreptamine
Streptomycin GA-10 O-2-Deoxy-2-(methylamino)-a-L-glucopyranosyl-(1→2)-O-5-deoxy-3-C-formyl-a-L-lyxofuranosyl-(1→4)-N,N’-bis(aminoiminomethyl)-D-streptamine
Spectinomycin GA-11 Decahydro-4a,7,9-trihydroxy-2-methyl-6,8-bis(methylamino)-4H-Pyrano(2,3-b)(1,4)benzodioxin-4-one
Hygromycin B GA-12 O-6-amino-6-deoxy-L-glycero-D-galacto-heptopyranosylidene-(1-2-3)-O-β-D-talopyranosyl-(1→5)-2-deoxy-N3-methyl-D-streptamine
Vancomycin GA-13 (1S,2R,18R,19R,22S,25R,28R,40S)-22-(2-Amino-2-oxoethyl)-48-{[2-O-(3-amino-2,3,6-trideoxy-3-methyl-α-L-lyxo-hexopyranosyl)-β-D-glucopyranosyl]oxy}-5,15-dichloro-2,18,32,35,37-pentahydroxy-19-[(N -methyl-D-leucyl)amino]-20,23,26,42,44-pentaoxo-7,13-dioxa-21,24,27,41,43-pentaazaoctacyclo[26.14.2.23,6.214,17.18,12.129,33.010,25.034,39]pentaconta-3,5,8(48),9,11,14,16,29(45),30,32,34,36,38,46,49-pentadecaene-40-carboxylic acid
Kanamycin A GA-14 O-3-Amino-3-deoxy-a-D-glucopyranosyl-(1→6)-O-[6-amino-6-deoxy-a-D-glucopyranosyl-(1→4)]-2-deoxy-D-streptamine
Neamine GA-15 2-Deoxy-4-O-(2,6-diamino-2,6-dideoxy-a-D-glucopyranosyl)-D-streptamine
Apramycin GA-16 4-O-[3a-Amino-6a-[(4-amino-4-deoxy-a-D-glucopyranosyl)oxy]-2,3,4,4ab,6,7,8aa-octahydro-8b-hydroxy-7b-(methylamino)pyranopyrano[3,2-b]pyran-2a-yl]-2-deoxy-D-streptamine
Oritavancin GA-17 (4”R)-22-O-(3-Amino-2,3,6-trideoxy-3-C-methyl-alpha-L-arabinohexopyranosyl)-N3”-(p-(p-chlorophenyl)benzyl)(1S,2R,18R,19R,22S,25R,28R,40S)-22-(2-Amino-2-oxoethyl)-48-{[2-O-(3-amino-2,3,6-trideoxy-3-methyl-α-L-lyxo-hexopyranosyl)-β-D-glucopyranosyl]oxy}-5,15-dichloro-2,18,32,35,37-pentahydroxy-19-[(N -methyl-D-leucyl)amino]-20,23,26,42,44-pentaoxo-7,13-dioxa-21,24,27,41,43-pentaazaoctacyclo[26.14.2.23,6.214,17.18,12.129,33.010,25.034,39]pentaconta-3,5,8(48),9,11,14,16,29(45),30,32,34,36,38,46,49-pentadecaene-40-carboxylic acid
Ribostamycin GA-18 O-2,6-Diamino-2,6-dideoxy-α-D-glucopyranosyl-(1→4)-O-[β-D-ribofuranosyl-(1→5)]-2-deoxy-D-streptamine
Azithromycin GA-19 2,6-dideoxy-3-C-methyl-3-O-methyl-α-L-ribo-hexopyranoside
Bleomycin A2/B2 GA-20 (βR)-N(α)-{[6-amino-2-((1S)-3-amino-1-{[(2S)-2,3-diamino-3-oxopropyl]amino}-3-oxopropyl)-5-methylpyrimidin-4-yl]carbonyl}-β-{2-O-[3-O-(aminocarbonyl)-α-D-mannopyranosyl]-α-L-gulopyranosyloxy}-N-[(1R,2S,3S)-5-({(1S,2R)-1-[({2-[4-({[3-(dimethylsulfonio)propyl]amino}carbonyl)-2,4′-bi-1,3-thiazol-2′-yl]ethyl}amino)carbonyl]-2-hydroxypropyl}amino)-3-hydroxy-4-methyl-5-oxopentan-2-yl]-L-histidinamide
Toyocamycin GA-21 4-Amino-7-(β-D-ribofuranosyl)-7H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile
Puromycin GA-22 6-Dimethylamino-9-(3′-(p-methoxy-L-phenylalanylamino)-beta-D-ribofuranosyl)-purine
Natamycin GA-23 16-(3-Amino-3,6-dideoxy-beta-D-mannopyranosyloxy)-5,6-epoxy-8,12,14-trihydroxy-26-methyl-2,10-dioxo-1-oxacyclohexacosa-3,17,19,21,23-pentaen-13-carboxylic acid

Examples

The anti-vancomycin antibody binds to vancomycin

The GlycoAntibiotic array was assayed with an anti-vancomycin antibody (5 μg/mL), followed by an anti-rabbit IgG (Cy3) antibody. The array was scanned with a microarray scanner at 532nm wavelength. Positive control showed binding signals as expected. The anti-vancomycin antibody binds explicitly to vancomycin.

Document

List of structures of glycopeptide antibiotics on the array (download the PDF)

Protocol & User Manual (download the manual)