Synthesis, purification, and properties of a peptide that enhances the activation of human [Glu1]plasminogen by tissue plasminogen activator and retards fibrin polymerization.
Solid phase synthesis of the hexapeptide, GPRVVE, which represents the amino terminal six amino acids of the alpha-chain of human fibrin, yielded a product that contained a modified glutamic acid. The nature of the modification was established as the Friedel-Crafts acylation product of the peptide and anisole, the latter reagent employed in the HF deblocking step. The anisoylated peptide selectively enhanced the activation rate of native [Glu1]plasminogen by recombinant tissue plasminogen activator, accelerated clot lysis, and retarded the polymerization of nascent fibrin.
Chibber
B A
BA
Department of Chemistry and Biochemistry, University of Notre Dame, Indiana.
Urano
S
S
Castellino
F J
FJ
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D006224:Cricetinae; D005337:Fibrin; D005971:Glutamates; D018698:Glutamic Acid; D006801:Humans; D008969:Molecular Sequence Data; D009391:Nephelometry and Turbidimetry; D010960:Plasminogen Activators; D010959:Tissue Plasminogen Activator / Q000494:pharmacology*
D005971:Glutamates; D018698:Glutamic Acid; D005337:Fibrin; D010960:Plasminogen Activators; D010959:Tissue Plasminogen Activator