Synthesis and characterization of sapecin and sapecin B.
Two insect defencins, sapecin and sapecin B, were chemically synthesized to confirm their structure and antibacterial activity and also to examine the possibility that these peptides bind to the same site on the large conductance calcium-activated potassium channel as charybdotoxin. Both synthetic peptides showed the same antibacterial activity as native sapecins, indicating that the synthetic peptides folded correctly in the chemical synthesis. Synthetic sapecins did not show an inhibitory effect on [125I]charybdotoxin binding to rat brain synaptic membranes, suggesting that sapecin B recognizes a different binding site from that of charybdotoxin despite the similar structural motif.
Kim
J I
JI
Mitsubishi Kasei Institute of Life Sciences, Tokyo, Japan.
Iwai
H
H
Kurata
S
S
Takahashi
M
M
Masuda
K
K
Shimada
I
I
Natori
S
S
Arata
Y
Y
Sato
K
K
D000595:Amino Acid Sequence; D000818:Animals; D000890:Anti-Infective Agents / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology; D001665:Binding Sites; D018999:Charybdotoxin; D004175:Diptera; D066298:In Vitro Techniques; D007301:Insect Hormones / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D019476:Insect Proteins; D008969:Molecular Sequence Data; D015221:Potassium Channels / Q000187:drug effects / Q000378:metabolism; D017510:Protein Folding; D051381:Rats; D012604:Scorpion Venoms / Q000378:metabolism; D013570:Synaptic Membranes / Q000187:drug effects / Q000378:metabolism
D000890:Anti-Infective Agents; D007301:Insect Hormones; D019476:Insect Proteins; D015221:Potassium Channels; D012604:Scorpion Venoms; C080667:sapecin B protein, Sarcophaga peregrina; D018999:Charybdotoxin; C057638:sapecin protein, Sarcophaga