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Originally published In Press as doi:10.1194/jlr.M500048-JLR200 on May 1, 2005

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Journal of Lipid Research, Vol. 46, 1512-1516, July 2005
Copyright © 2005 by American Society for Biochemistry and Molecular Biology

Peptide inhibitor of pancreatic lipase selected by phage display using different elution strategies

M. Lunder1,*, T. Bratkovic*,{dagger}, S. Kreft* and B. Strukelj*,§

* Department of Pharmaceutical Biology, Faculty of Pharmacy, Ljubljana, Slovenia
{dagger} Lek Pharmaceuticals d.d., Ljubljana, Slovenia
§ Jozef Stefan Institute, Ljubljana, Slovenia

Published, JLR Papers in Press, May 1, 2005. DOI 10.1194/jlr.M500048-JLR200

1 To whom correspondence should be addressed. e-mail: mojca.lunder{at}ffa.uni-lj.si

Interference with fat hydrolysis results in the reduced use 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 an attempt to select peptides with affinity for the surface of pancreatic lipase and potential inhibitory activity, a random, cyclic heptapeptide phage-displayed library was used. Five independent selections, differing in elution step, were performed. In three selection protocols, a sequential elution strategy was applied in anticipation of improving the selection of high-affinity clones. Four heptapeptides with the highest affinity, seemingly 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 an apparent inhibition constant of 16 µM.

Abbreviations: Ki(app), apparent inhibition constant; PBST, PBS containing Tween 20; pfu, plaque-forming units; THL, tetrahydrolipstatin

Supplementary key words sequential elution • obesity • peptide drug leads


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