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conference paper
Chemical synthesis and functional characterization of melittin-TASP molecules
1994
Innovation and perspectives in solid phase synthesis : peptides, proteins and nucleic acids : biological and biomedical applications : collected papers, third international symposium
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)]
Type
conference paper
Authors
Publication date
1994
Published in
Innovation and perspectives in solid phase synthesis : peptides, proteins and nucleic acids : biological and biomedical applications : collected papers, third international symposium
Start page
485
End page
488
Peer reviewed
REVIEWED
EPFL units
Available on Infoscience
February 9, 2006
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