Molecular aggregation and conformational change of wasp venom mastoparan as induced by salt in aqueous solution

• Published in: Biochimica et biophysica acta Vol. 802; no. 2; pp. 157 - 161
• Main Authors: Higashijima, Tsutomu, Wakamatsu, Kaori, Saito, Kazuki, Fujino, Masahiko, Nakajima, Terumi, Miyazawa, Tatsuo
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 28.11.1984; Elsevier; North-Holland
• Subjects: Analytical, structural and metabolic biochemistry; Biological and medical sciences; Conformational change; Fundamental and applied biological sciences. Psychology; Mastoparan; Miscellaneous; Proteins; Salt effect; Wasp venom; Wasp venom; Salt effect; Mastoparan; Conformational change; Radiolabelling; Peptides; Arthropoda; Insecta; Venom; Molecular association; NMR spectrometry; Helical structure; Invertebrata; Circular dichroism; Conformational transition
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/0304-4165(84)90156-9

The effect of salt on molecular aggregation and conformation has been studied of mastoparan from wasp venom, a tetradecapeptide causing the degranulation of mast cells. The 270 MHz 1H-NMR and CD spectra of mastoparan in solution have been analyzed. On addition of salt at high concentration in aqueous solution, the monomeric form of mastoparan in largely unordered conformation is converted to the molecular aggregate (probably tetramer) with a largely α-helical conformation. The molecular aggregation of mastoparan depends on pH and ionic strength, but not on the kind of counter anion, in contrast to the case with melittin from bee venom.