Kringle 5 peptide-albumin conjugates with anti-migratory activity

Roger Léger; Corinne Benquet; Xicai Huang; Omar Quraishi; Pieter van Wyk; Dominique Bridon

doi:10.1016/j.bmcl.2003.12.025

Kringle 5 peptide-albumin conjugates with anti-migratory activity

Bioorg Med Chem Lett. 2004 Feb 23;14(4):841-5. doi: 10.1016/j.bmcl.2003.12.025.

Authors

Roger Léger¹, Corinne Benquet, Xicai Huang, Omar Quraishi, Pieter van Wyk, Dominique Bridon

Affiliation

¹ Research Department, ConjuChem Inc., 225 President-Kennedy Ave., Suite 3950, Montréal, QC, H2X 3Y8 Canada. leger@conjuchem.com

PMID: 15012978
DOI: 10.1016/j.bmcl.2003.12.025

Abstract

Three peptide fragments of the kringle 5 region of plasminogen and their respective N- and C-terminus maleimido derivatives conjugated to Cys34 of human serum albumin were evaluated in vitro using a human umbilical vein endothelial cell (HUVEC) migration assay and a human plasma stability assay. The N-terminus maleimido derivative of the 64 to 74 segment of kringle 5 conjugated to human serum albumin possessed remarkable anti-migratory activity.

MeSH terms

Amino Acid Sequence
Cell Movement / drug effects*
Cross-Linking Reagents / chemistry*
Cross-Linking Reagents / pharmacology*
Endothelium, Vascular / cytology
Endothelium, Vascular / drug effects
Humans
Kringles*
Molecular Sequence Data
Peptide Fragments / chemistry*
Peptide Fragments / genetics
Peptide Fragments / pharmacology*
Plasminogen / chemistry
Plasminogen / genetics
Plasminogen / pharmacology
Serum Albumin / chemistry*

Substances

Cross-Linking Reagents
Peptide Fragments
Serum Albumin
Plasminogen