Demonstration that [A103,106,108] antistasin 93-119 inhibits the specific binding of antistasin to sulfatide [Gal(3-SO4)beta 1-1Cer].
Antistasin is a 119 amino acid heparin-binding protein from the leech Haementaria officinalis which has anticoagulant and antimetastatic properties. A series of peptides representing the basic amino acid-rich domains of the amino- and carboxyl-terminal regions of the inhibitor were synthesized by solid-phase peptide chemistry and their ability to bind sulfated glycolipids was investigated. The findings show that [A103,106,108] antistasin 93-119 has high affinity for sulfatide and inhibits the specific interaction of whole antistasin with [Gal(3-SO4)beta 1-1Cer]. We conclude that the 93-119 region is a critical domain that mediates the interaction of antistasin with sulfated glycolipids.
Brankamp
R G
RG
Marion Merrell Dow Research Institute, Cincinnati, Ohio 45215.
Manley
G D
GD
Owen
T J
TJ
Krstenansky
J L
JL
Smith
P L
PL
Cardin
A D
AD
D000595:Amino Acid Sequence; D000818:Animals; D001667:Binding, Competitive; D007447:Invertebrate Hormones / Q000378:metabolism* / Q000494:pharmacology*; D007700:Kinetics; D007865:Leeches; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000494:pharmacology*; D010455:Peptides / Q000138:chemical synthesis / Q000494:pharmacology; D011485:Protein Binding; D012471:Salivary Proteins and Peptides / Q000378:metabolism; D013433:Sulfoglycosphingolipids / Q000378:metabolism*
C071876:(A103,106,108)antistasin (93-119); D007447:Invertebrate Hormones; D010446:Peptide Fragments; D010455:Peptides; D012471:Salivary Proteins and Peptides; D013433:Sulfoglycosphingolipids; C053155:antistasin