Submitted on February 4, 2005
Revised on April 14, 2005
Accepted on April 18, 2005
Peptide inhibitor of pancreatic lipase selected by phage display using different elution strategies
M. Lunder, T. Bratkovic, S. Kreft, and B. Štrukelj
Department of Pharmaceutical Biology, Faculty of Pharmacy, Ljubljana SI-1000
Corresponding Author: mojca.lunder{at}ffa.uni-lj.si
Interference with fat hydrolysis results in reduced utilisation of ingested lipids. Inhibition of pancreatic lipase reduces the efficiency of fat absorption in the small intestine and thereby initiates modest long-term reduction in body weight. In attempt to select peptides with affinity for the surface of pancreatic lipase and potential inhibitory activity, random cyclic heptapeptide phage displayed library was used. Five independent selections differing in elution step were performed. In three selection protocols sequential elution strategy was applied in anticipation of improving the selection of high affinity clones. Four heptapeptides with the highest affinity for pancreatic lipase were selected, synthesized and characterized for their capacity to inhibit enzyme function. Although no clear consensus among the sequenced peptides was found, one of the selected peptides inhibited pancreatic lipase with Ki(app) of 16 µM.
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