1228577-19-2

Upstream product

• 28224-73-9 1,3:4,6-di-O-benzylidene-D-mannitol 
• 1228577-18-1 1,3,4,6-di-O-benzylidene-2,5-O-isopropylidene-D-mannitol 

Downstream Products

• 1228577-20-5 1,3-O-benzylidene-2,5-O-isopropylidene-4-O-methoxymethyl-D-mannitol 
• 1228577-17-0 5,7-O-benzylidene-1,2-dideoxy-3,6-O-isopropylidene-4-O-(methoxymethyl)-D-mannohept-1-enitol 
• 1228577-21-6 1,3-O-benzylidene-2,5-O-isopropylidene-4-O-(methoxymethyl)-D-glycero-D-mannoheptitol 
• 1228577-22-7 1,3-O-benzylidene-2,5-O-isopropylidene-4-O-(methoxymethyl)-D-glycero-D-galactoheptitol 
• 1228577-26-1 2,3,5-tri-O-p-methoxybenzyl-1,4-dideoxy-1,4-[[[2S,3S,4R,5R,6R]-2,5-isopropylidene-4,6,7-tri-O-methoxymethyl-3-(sulfooxy)heptyl]-(R)-epi-sulfoniumylidine]-D-arabinitol inner salt 

Relevant academic research and scientific papers

SALACINOL AND PONKORANOL HOMOLOGUES, DERIVATIVES THEREOF, AND METHODS OF SYNTHESIZING SAME

Salacinol and ponkoranol homologues, derivatives thereof and methods of synthesizing and using said homologies and derivatives. The derivatives include stereoisomers, de-O-sulfonated compounds and congeners of the naturally occurring homologues. Some of the derivatives exhibit enhanced glucosidase inhibitory bioactivity in comparison to the naturally occurring compounds which have been isolated from salacia reticulata.

Synthesis of a biologically active isomer of kotalanol, a naturally occurring glucosidase inhibitor

The syntheses of an isomer of kotalanol, a naturally occurring glucosidase inhibitor, and of kotalanol itself are described. The target compounds were synthesized by nucleophilic attack of PMB-protected 1,4-anhydro-4-thio-d-arabinitol at the least hindered carbon atom of two 1,3-cyclic sulfates, which were synthesized from d-mannose. Methoxymethyl ether and isopropylidene were chosen as protecting groups. The latter group was critical to ensure the facile deprotection of the coupled products in a one-step sequence to yield kotalanol and its isomer. The stereoisomer of kotalanol, with the opposite stereochemistry at the C-6′ stereogenic centre, inhibited the N-terminal catalytic domain of intestinal human maltase glucoamylase (ntMGAM) with a Ki value of 0.20 ± 0.02 μM; this compares to a Ki value for kotalanol of 0.19 ± 0.03 μM. The results indicate that the configuration at C-6′ is inconsequential for inhibitory activity against this enzyme.