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Chemical synthesis and functional characterization of melittin-TASP molecules

Horst Vogel
1994
Conference paper
Abstract

A symposium report. The total synthesis of melittin-TASP, T4-(4a26) (TASP = template assembled synthetic proteins) is described together with its structural and ion-channel forming properties in planar lipid bilayers. A voltage-dependent channel activity is obsd. upon application of pos. voltage on the side of protein addn. This rectification is indicative of four helixes structurally forced into an unidirectional orientation within the channel aggregate. Melittin-TASPs show a two orders of magnitude higher potency in permeabilizing the bilayer membranes than native melittin. [on SciFinder (R)]

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