New methods of isolating bee venom peptides
β Scribed by Barbara E.C. Banks; Chris E. Dempsey; Frederick L. Pearce; Charles A. Vernon; Teresa E. Wholley
- Book ID
- 102629589
- Publisher
- Elsevier Science
- Year
- 1981
- Tongue
- English
- Weight
- 470 KB
- Volume
- 116
- Category
- Article
- ISSN
- 0003-2697
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## Abstract The circular dichroism (CD) and ^1^Hβnmr properties of peptide 401, a bee venom component with 22 amino acid residues and two disulfide bridges, have been studied under a variety of conditions and compared with those of the structurally related octadecapeptide apamin. The major componen
**Potential value in the therapy of rheumatism and other inflammation processes** could attach to the MCD peptide from bee venom if it were available in larger quantities. The peptide consists of 22 amino acids and contains two disulfide bridges. Its first total synthesis has now been accomplished.
In aqueous solution, melittin structure, investigated by CD and 'H-nmr, depends on pH and ionic composition, which also regulate the aggregation state of the peptide. When interacting with phospholipids, however, melittin exhibits a right-handed helical conformation without any evidence of oligomeri