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Self-Assembly of Amphiphilic Peptides

English title Self-Assembly of Amphiphilic Peptides
Applicant Meier Wolfgang
Number 115876
Funding scheme Project funding
Research institution Physikalische Chemie Departement Chemie Universität Basel
Institution of higher education University of Basel - BS
Main discipline Physical Chemistry
Start/End 01.04.2007 - 31.03.2010
Approved amount 191'531.00
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Keywords (8)

AMPHIPHILES; PEPTIDES; SELF-ASSEMBLY; lytotropic MESOPHASES; SOFT MATTER; membranes; lyotropic mesophases; vesicles

Lay Summary (English)

Lay summary
In this project we will synthesize new amphiphilic peptides based on a hydrophobic gramicidin A (g.A) building block. These peptides are designed to self-assemble in aqueous media into well-defined superstructures and lyotropic mesophases. By exchanging individual amino acids along the peptide sequence it will be possible to introduce well-defined secondary interactions that can be used to influence the self-assembly of the systems. A particularly interesting aspect arises from the fact that the new g-A based amphiphiles allow complementing the experiments by molecular dynamics simulations. Therefore we regard these amphiphilic peptides as ideal model systems to develop a deeper understanding of how self-organization, the resulting structures and interfacial patterns are controlled by the (molecular) architecture of the building blocks. We expect to obtain functional, environmentally responsive materials that could provide new interfaces between synthetic and living matter. In this project we plan a basic characterization of a series of model g.A amphiphiles that provides a solid platform for future applications of these new functional and responsive materials. In this context we focus on the influence of molecular constitution, architecture, molar mass and charge of the individual hydrophilic and hydrophobic building blocks on structure and dynamics of the resulting self-organized systems in diluted and concentrated aqueous solution and at surfaces. Presence of monovalent ions, organic solvents or pH changes are expected to induce transitions in the secondary structure of the basic peptides that will significantly influence the structure and dynamics of the self-assembled superstructures. In addition these amphiphiles offer the possibility to introduce different well-defined functional groups that can be used to prepare functional, solid supported membranes by controlled dimerization of ‘single-stranded’ peptide motifs. The potential of such surface structures for cell-adhesion and biomineralization will be investigated.
Direct link to Lay Summary Last update: 21.02.2013

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Associated projects

Number Title Start Funding scheme
107426 Self-Assembly of Amphiphilic Blockcopolypeptides 01.04.2005 Project funding