Nuclear magnetic resonance studies on conformation and stability of mastoparan in methanol.
Yoshinori MiuraPublished in: Journal of peptide science : an official publication of the European Peptide Society (2021)
Mastoparan is a small peptide composed of 14 amino acid residues found in wasp venom. It penetrates into cytoplasm through the cell membranes and then binds to a G protein to stimulate the release of histamine. Conformation and its thermal stability of mastoparan from Vespula lewisi (MP) in methanol are investigated by using proton nuclear magnetic resonance (NMR) spectroscopy. On the basis of data on NOESY cross peaks, spin-spin coupling constants between an amide proton (NH) and an α-proton, NH chemical shift analyses, and temperature dependence of integrated intensity of NH resonance lines, we found that MP forms the helix between the 5th and 12th residues at low temperatures and the helix segment is maintained even at 54°C. This conformation is similar to that of MP bound to detergent micelles, and hence, methanol is considered to be appropriate as a membrane mimetic for MP. In connection with the function of the venom peptide, significance of high stability of the helical conformation is discussed.
Keyphrases
- room temperature
- magnetic resonance
- molecular dynamics simulations
- crystal structure
- carbon dioxide
- amino acid
- ionic liquid
- contrast enhanced
- electron transfer
- drug delivery
- density functional theory
- single cell
- perovskite solar cells
- magnetic resonance imaging
- cell therapy
- dna binding
- stem cells
- electronic health record
- high intensity
- machine learning
- artificial intelligence
- case control
- drug release
- hyaluronic acid
- quantum dots