Synthesis of an oxime-linked neoglycopeptide with glycosylation-dependent activity similar to its native counterpart

Marcaurelle, Lisa A.; Rodriguez, Elena C.; Bertozzi, Carolyn R.

doi:10.1016/s0040-4039(98)01831-0

Cited by 54 publications

(46 citation statements)

References 19 publications

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“…The chemical nature of the peptide-sugar connection does not seem to play a role in the activity either. Drosocin variants, in which the native classical O-linked sugars in h-anomeric configuration are replaced with oxime-linked carbohydrates, work equally well [51,52].…”

Section: Insect Antibacterial Peptide Familiesmentioning

confidence: 98%

Antibacterial peptides isolated from insects

2000

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Section: Insect Antibacterial Peptide Familiesmentioning

confidence: 98%

Antibacterial peptides isolated from insects

2000

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“…sugars are replaced with oxime-linked carbohydrates, work equally well [41,42]. Another typical member of the family, the 20-mer pyrrhocoricin, was isolated from the European sap-sucking bug Pyrrhocoris apterus [43].…”

Section: Currently Known Members Of the Short Proline-rich Peptide Fmentioning

confidence: 99%

The short proline-rich antibacterial peptide family

Ötvös¹

2002

Cellular and Molecular Life Sciences (CMLS)

194

201

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From the many peptide families that are induced upon bacterial infection and can be isolated from all classes of animals, the short, proline-rich antibacterial peptides enjoy particular interest. These molecules were shown to inactivate an intracellular biopolymer in bacteria without destroying or remaining attached to the bacterial cell membrane, and as such emerged as viable candidates for the treatment of mammalian infections. These peptides were originally isolated from insects, they kill mostly gram-negative bacteria with high efficiency and they show structural similarities with longer insect- and mammal-derived antimicrobial peptides. However, while the distant relatives appear to carry multiple functional domains, apidaecin, drosocin, formaecin and pyrrhocoricin consist of only minimal determinants needed to penetrate across the cell membrane and bind to the target biopolymer. These peptides appear to inhibit metabolic processes, such as protein synthesis or chaperone-assisted protein folding. Pyrrhocoricin derivatives protect mice from experimental infections in vivo, suggesting the utility of modified analogs in the clinical setting. Sequence variations of the target protein at the peptide-binding site may allow the development of new peptide variants that kill currently unresponsive strains or species.

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“…25 As well, the use of C(2)-azido halides resulted in 67% yield however with low selectivity (α:β = 3:1); α-only selectivity has been previously reported through the use of an expensive phase transfer catalyst and a difficult to fashion β-chloride. 26 Subsequent conversion of 26 into N -acetylated 27 (81%) was achieved by removal of the benzylidene group followed by acetylation. Hydrolysis of the known compound 27 would reveal the free α-aminoxy glycoside 28 .…”

Section: Resultsmentioning

confidence: 99%

“…Hydrolysis of the known compound 27 would reveal the free α-aminoxy glycoside 28 . 25,26 Andreana and coworkers were able to conjugate 28 to the modified version of immunostimulant PS A1 to produce 29 (Scheme 5) for use as potential vaccine. 26e On other the hand, Bertozzi and coworkers conjugated 28 to a polymer scaffold containing pendant ketone to generate 30 (Scheme 5) for use to mimic the MUC1 mucin of epithelial cells.…”

Section: Resultsmentioning

confidence: 99%

Utilization of bench-stable and readily available nickel(II) triflate for access to 1,2-cis-2-aminoglycosides

Sletten

Ramadugu

Nguyen

2016

Carbohydrate Research

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The utilization of substoichiometric amounts of commercially available nickel(II) triflate as an activator in the reagent-controlled glycosylation reaction for the stereoselective construction of biologically relevant targets containing 1,2-cis-2-amino glycosidic linkages is reported. This straightforward and accessible methodology is mild, operationally simple and safe through catalytic activation by readily available Ni(OTf)2 in comparison to systems employing our previously in-house prepared Ni(4-F-PhCN)4(OTf)2. We anticipate that the bench-stable and inexpensive Ni(OTf)2, coupled with little to no extra laboratory training to set up the glycosylation reaction and no requirement of specialized equipment, should make this methodology be readily adopted by non-carbohydrate specialists. This report further highlights the efficacy of Ni(OTf)2 to prepare several bioactive motifs, such as blood type A-type V and VI antigens, heparin sulfate disaccharide repeating unit, aminooxy glycosides, and α-GalNAc-Serine conjugate, which cannot be achieved in high yield and α-selectivity utilizing in-house prepared Ni(4-F-PhCN)4(OTf)2 catalyst. The newly-developed protocol eliminates the need for the synthesis of Ni(4-F-PhCN)4(OTf)2 and is scalable and reproducible. Furthermore, computational simulations in combination with 1H NMR studies analyzed the effects of various solvents on the intramolecular hydrogen bonding network of tumor-associated mucin Fmoc-protected GalNAc-threonine amino acid antigen derivative, verifying discrepancies found that were previously unreported.

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Synthesis of an oxime-linked neoglycopeptide with glycosylation-dependent activity similar to its native counterpart

Cited by 54 publications

References 19 publications

Antibacterial peptides isolated from insects

Antibacterial peptides isolated from insects

The short proline-rich antibacterial peptide family

Utilization of bench-stable and readily available nickel(II) triflate for access to 1,2-cis-2-aminoglycosides

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