Chemical synthesis and functional characterization of melittin-TASP molecules

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)]

Published in:
Innovation and perspectives in solid phase synthesis : peptides, proteins and nucleic acids : biological and biomedical applications : collected papers, third international symposium, 485-488

 Record created 2006-02-09, last modified 2018-01-27

Rate this document:

Rate this document:
(Not yet reviewed)