Journal
GLYCOCONJUGATE JOURNAL
Volume 26, Issue 2, Pages 133-140Publisher
SPRINGER
DOI: 10.1007/s10719-008-9171-3
Keywords
Peptide:N-glycanase; Haloacetamidyl oligosaccharide; Inhibitor
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Funding
- Chemical Biology program in RIKEN
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A series of glycosyl haloacetamides were synthesized as potential inhibitors of cytoplasmic peptide:N-glycanase (PNGase), an enzyme that removes N-glycans from misfolded glycoproteins. Chloro-, bromo-, and iodoacetamidyl chitobiose and chitotetraose derivatives exhibited a significant inhibitory activity. No inhibitory activity was observed with of fluoroacetamididyl derivatives. Moreover, N-acetylglucosamine derivatives, beta-chloropropionamidyl chitobiose, and chloroacetamidyl cellooligosaccharide derivatives did not show any activity. These results underscore the importance of the N-acetyl groups of chitobiose for PNGase recognition. In addition, reactivity and position of the leaving group at the reducing end are also important factors.
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