Synthesis and characterization of sapecin and sapecin B
- 4 April 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 342 (2) , 189-192
- https://doi.org/10.1016/0014-5793(94)80498-2
Abstract
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.Keywords
This publication has 13 references indexed in Scilit:
- Inhibition of the Ca2v+‐activated K+‐channel by sapecin B, an insect antibacterial proteinFEBS Letters, 1994
- Purification, sequence and antibacterial activity of two novel sapecin homologues from Sarcophaga embryonic cells: similarity of sapecin B to charybdotoxinBiochemical Journal, 1993
- Synthetic charybdotoxin-iberiotoxin chimeric peptides define toxin binding sites on calcium-activated and voltage-dependent potassium channelsBiochemistry, 1993
- Refined Structure of Charybdotoxin: Common Motifs in Scorpion Toxins and Insect DefensinsScience, 1991
- 1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecinFEBS Letters, 1990
- Role of surface electrostatics in the operation of a high-conductance calcium-activated potassium channelBiochemistry, 1989
- Functional modification of calcium-activated potassium channel by trimethyloxoniumBiochemistry, 1989
- Purification, sequence, and model structure of charybdotoxin, a potent selective inhibitor of calcium-activated potassium channels.Proceedings of the National Academy of Sciences, 1988
- Mechanism of charybdotoxin block of the high-conductance, Ca2+-activated K+ channel.The Journal of general physiology, 1988
- Charybdotoxin, a protein inhibitor of single Ca2+-activated K+ channels from mammalian skeletal muscleNature, 1985