Inhibitory activity of sulphoglycolipid derivatives towards pancreatic trypsin

Amphipathic sulpholipids have been shown to inhibit pancreatic serine prote ases due to their detergent-like properties. To evaluate the structural req uirement for this inhibitory activity, we examined the effects of various d erivatives of sulphoglycolipids, some of which were prepared by deacylation with sphingolipid ceramide N-deacylase, followed by acylation with acyl ch loride, on the activity of pancreatic trypsin. Both deacylated sulphatides and seminolipids exhibited inhibitory activity towards trypsin without any requirement for solubilisation and preincubation. On the other hand, strong er inhibition was observed for acylated sulphatides than for deacylated one s, but increasing the chain length of the fatty acid moiety resulted in the need for a solubilisation agent and preincubation in order to achieve maxi mal inhibitory activity. The structural isomers of sulphoglycolipids, such as (ISO3)-S-6-GalCer, and phytosphingosine- and diglyceride-containing sulp hoglycolipids, showed similar inhibitory activity, indicating the involveme nt of sulphate and hydrophobic groups, irrespective of the fine structure, in the inhibition. Among the sulphoglycolipids examined, (IISO3)-S-3-LacCer was found to exhibit the highest inhibitory activity.