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 N-terminus maleimido derivative of the 64 to 74 segment of kringle 5 conjugated to human serum albumin possessed remarkable anti-migratory activity.
Léger
Roger
R
Research Department, ConjuChem Inc., 225 President-Kennedy Ave., Suite 3950, Montréal, QC, H2X 3Y8 Canada. leger@conjuchem.com
Benquet
Corinne
C
Huang
Xicai
X
Quraishi
Omar
O
van Wyk
Pieter
P
Bridon
Dominique
D
D000595:Amino Acid Sequence; D002465:Cell Movement / Q000187:drug effects*; D003432:Cross-Linking Reagents / Q000737:chemistry* / Q000494:pharmacology*; D004730:Endothelium, Vascular / Q000166:cytology / Q000187:drug effects; D006801:Humans; D018082:Kringles; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics / Q000494:pharmacology*; D010958:Plasminogen / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology; D012709:Serum Albumin / Q000737:chemistry*
D003432:Cross-Linking Reagents; D010446:Peptide Fragments; D012709:Serum Albumin; D010958:Plasminogen