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Kringle 5 peptide-albumin conjugates with anti-migratory activity.
- Source :
-
Bioorganic & medicinal chemistry letters [Bioorg Med Chem Lett] 2004 Feb 23; Vol. 14 (4), pp. 841-5. - Publication Year :
- 2004
-
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.
- Subjects :
- Amino Acid Sequence
Endothelium, Vascular cytology
Endothelium, Vascular drug effects
Humans
Molecular Sequence Data
Peptide Fragments genetics
Plasminogen chemistry
Plasminogen genetics
Plasminogen pharmacology
Cell Movement drug effects
Cross-Linking Reagents chemistry
Cross-Linking Reagents pharmacology
Kringles
Peptide Fragments chemistry
Peptide Fragments pharmacology
Serum Albumin chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0960-894X
- Volume :
- 14
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Bioorganic & medicinal chemistry letters
- Publication Type :
- Academic Journal
- Accession number :
- 15012978
- Full Text :
- https://doi.org/10.1016/j.bmcl.2003.12.025