ArticleProtein science : a publication of the Protein Society1994
Template-assembled melittin: structural and functional characterization of a designed, synthetic channel-forming protein.
Article in Protein science : a publication of the Protein Society, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 61 citations in OpenAlex.
- Conformational Fine-Tuning of Pore-Forming Peptide Potency and Selectivity.Journal of the American Chemical Society · 2015Article
- Gain-of-function analogues of the pore-forming peptide melittin selected by orthogonal high-throughput screening.Journal of the American Chemical Society · 2012Article
- Multivalent display of the antimicrobial peptides BP100 and BP143.Beilstein journal of organic chemistry · 2012Article
- Applications of biological pores in nanomedicine, sensing, and nanoelectronics.Current opinion in biotechnology · 2010Review
- Using ion channel-forming peptides to quantify protein-ligand interactions.Journal of the American Chemical Society · 2008Article
- Synthetic, biologically active amphiphilic peptides.Chemistry & biodiversity · 2007Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Template-assembled proteins (TASPs) comprising 4 peptide blocks, each of either the natural melittin sequence (melittin-TASP) or of a truncated melittin sequence (amino acids 6-26, melittin6-26-TASP), C-terminally linked to a (linear or cyclic) 10-amino acid template were synthesized and characterized, structurally by CD, by fluorescence spectroscopy, and by monolayer experiments, and functionally, by electrical conductance measurements on planar bilayers and release experiments on dye-loaded vesicles. Melittin-TASP and the truncated analogue preferentially adopt alpha-helical structures in methanol (56% and 52%, respectively) as in lipid membranes. Unlike in methanol, the melittin-TASP self-aggregates in water. On an air-water interface, the differently sized molecules can be self-assembled and compressed to a compact structure with a molecular area of around 600 A2, compatible with a 4-helix bundle preferentially oriented perpendicular to the interface. The proteins reveal a strong affinity for lipid membranes. A partition coefficient of 1.5 x 10(9) M-1 was evaluated from changes of the Trp fluorescence spectra of the TASP in water and in the lipid bilayer. In planar lipid bilayers, TASP molecules are able to form defined ion channels, exhibiting a small single-channel conductance of 7 pS (in 1 M NaCl). With increasing protein concentration in the lipid bilayer, additional, larger conductance states of up to 1 nS were observed. These states are likely to be formed by aggregated TASP structures as inferred from a strongly voltage-dependent channel activity on membranes of large area. In this respect, melittin-TASP reveals channel features of the native peptide, but with a considerably lower variation in the size of the channel states. Compared to the free peptide, template-assembled melittin has a much higher membrane activity: it is about 100 times more effective in channel formation and 20 times more effective in releasing dye molecules from lipid vesicles. This demonstrates that the lytic properties are not solely related to channel formation.
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