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Biophysical Journal 63: 1536-1543 (1992)
© 1992 the Biophysical Society

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A synthetic analogue of melittin aggregates in large oligomers.

E John and F Jähnig

Max-Planck-Institut für Biologie, Tübingen, Germany.

ABSTRACT

An analogue of melittin synthesized in the group of E. T. Kaiser (DeGrado, W. F., F. J. Kezdy, and E. T. Kaiser. 1981. J. Am. Chem. Soc. 103:679-681) was investigated by Raman spectroscopy and fluorescence anisotropy decay. In water, the analogue is completely alpha-helical and aggregates in large oligomers of about 50 monomers. In vesicle membranes, it undergoes orientational fluctuations similar to melittin. The most significant difference from melittin, therefore, is the formation of straight helixes and their aggregation in large oligomers in water. We interpret this as a consequence of the lacking proline residue in the analogue. We, furthermore, hypothesize that the increased tendency for aggregation causes the increased hemolytic activity of the analogue.




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Copyright © 1992 by the Biophysical Society.