Kringle 5 peptide-albumin conjugates with anti-migratory activity

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...

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Bibliographic Details
Published in:Bioorganic & medicinal chemistry letters 2004-02, Vol.14 (4), p.841-845
Main Authors: LEGER, Roger, BENQUET, Corinne, XICAI HUANG, QURAISHI, Omar, VAN WYK, Pieter, BRIDON, Dominique
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Antineoplastic agents
Biological and medical sciences
Cell Movement - drug effects
Cross-Linking Reagents - chemistry
Cross-Linking Reagents - pharmacology
Endothelium, Vascular - cytology
Endothelium, Vascular - drug effects
General aspects
Humans
Kringles
Medical sciences
Molecular Sequence Data
Peptide Fragments - chemistry
Peptide Fragments - genetics
Peptide Fragments - pharmacology
Pharmacology. Drug treatments
Plasminogen - chemistry
Plasminogen - genetics
Plasminogen - pharmacology
Serum Albumin - chemistry
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Summary: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.
ISSN:0960-894X
1464-3405
DOI:10.1016/j.bmcl.2003.12.025