Chemical synthesis of gamma-echistatin analogues: elucidation of status of C-terminal (45-49).
Three analogues of gamma-echistatin, des(45-49)-gamma-echistatin, des(46-49)-gamma-echistatin and des(47-49)-gamma-echistatin, were synthesized by solid-phase methodology and their biological activities were measured and compared. The results reveal that without the C-terminal (45-49) of gamma-echistatin, the folding of the protein to the final active structure is not interfered with and Lys-45 influences the inhibition of platelet aggregation.
Chen
P Y
PY
Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
Wu
S H
SH
Wang
K T
KT
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D036341:Intercellular Signaling Peptides and Proteins; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D010455:Peptides; D010974:Platelet Aggregation / Q000187:drug effects*; D010975:Platelet Aggregation Inhibitors / Q000494:pharmacology*; D011487:Protein Conformation; D017510:Protein Folding; D016415:Sequence Alignment; D013329:Structure-Activity Relationship; D014757:Viper Venoms / Q000737:chemistry*
D036341:Intercellular Signaling Peptides and Proteins; D010446:Peptide Fragments; D010455:Peptides; D010975:Platelet Aggregation Inhibitors; D014757:Viper Venoms; C057986:echistatin