Studies of the interaction of the maltose-binding protein of Escherichia coli, a closed-groove binder, with 4,6-O-ethylidenemalto-oligosaccharides (dp 2-5) and its regioselective labelling with 3-azibutyl 1-thio-α-(6-3H)maltoside

Article abstract of DOI:10.1016/S0008-6215(00)90995-9

Four malto-oligosaccharides (dp 2-5), each with 4,6-O-ethylidene group on the glucosyl unit at the non-reducing terminus, were synthesised and used to prove that the maltose-binding protein (MBP) of E. coli is a closed-groove binder, α-D-Glucosylation of 3-azibutyl 1-thio-α-D-(6-³H)glucopyranoside yielded a ³H-labelled, photolabile 1-thiomaltoside derivative that was used to chemically modify the binding site of MBP. The ³H-labelled peptide containing 83% of the total radioactivity, which was isolated after tryptic cleavage of the modified MBP and sequenced, is part of the closed end of the MBP groove. Four malto-oligosaccharides (dp 2-5), each with a 4,6-O-ethylidene group on the glucosyl unit at the non-reducing terminus, were synthesised and used to prove that the maltose-binding protein (MBP) of E. coli is a closed-groove binder, α-D-Glucosylation of 3-azibutyl 1-thio-α-D-(6-³H)glucopyranoside yielded a ³H-labelled, photolabile 1-thiomaltoside derivative that was used to chemically modify the binding site of MBP. The ³H-labelled peptide containing 83% of the total radioactivity, which was isolated after tryptic cleavage of the modified MBP and sequenced, is part of the closed end of the MBP groove.