New analogues of laminin active fragment YIGSR: synthesis and biological activity in vitro and in vivo.

Abstract

Eleven analogues of the laminin pentapeptide amide fragment Tyr-Ile-Gly-Ser-Arg-NH2 (YIGSR-NH2) corresponding to a B1 chain fragment of the glycoprotein laminin have been synthesized by the solid phase method, and their biological activity has been studied in vitro by a cell adhesion assay: all of them inhibited the adhesion of LLC tumor cells to laminin. The analogues were found to be more resistant to enzymatic degradation in human serum than YIGSR-NH2 itself. Analogue DatIGSHar-NH2 was selected for an experimental pulmonary metastasis assay in vivo: it had higher antimetastatic activity than YIGSR-NH2.

• Authors: Ewa Witkowska, Alicja Oriowska, Jan Izdebski, Jan Salwa, Joanna Wietrzyk, Adam Opolski
• Journal: Journal of peptide science : an official publication of the European Peptide Society (J Pept Sci) Vol. 10 Issue 5 Pg. 285-90 (May 2004) ISSN: 1075-2617 [Print] England
• PMID: 15160840 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Antineoplastic Agents
• Laminin
• Oligopeptides
• tyrosyl-isoleucyl-glycyl-seryl-arginine

Topics

• Animals
• Antineoplastic Agents (administration & dosage, chemical synthesis, chemistry, pharmacology)
• Cell Adhesion (drug effects)
• Cell Line, Tumor
• Drug Design
• Humans
• Laminin (chemistry)
• Male
• Melanoma, Experimental (drug therapy)
• Mice
• Molecular Structure
• Oligopeptides (administration & dosage, chemical synthesis, chemistry, pharmacology)
• Structure-Activity Relationship