Amyloid inspired self-assembled peptide nanofibers
Deniz Tekin, E.
Please cite this item using this persistent URLhttp://hdl.handle.net/11693/21306
Amyloid peptides are important components in many degenerative diseases as well as in maintaining cellular metabolism. Their unique stable structure provides new insights in developing new materials. Designing bioinspired self-assembling peptides is essential to generate new forms of hierarchical nanostructures. Here we present oppositely charged amyloid inspired peptides (AIPs), which rapidly self-assemble into nanofibers at pH 7 upon mixing in water caused by noncovalent interactions. Mechanical properties of the gels formed by self-assembled AIP nanofibers were analyzed with oscillatory rheology. AIP gels exhibited strong mechanical characteristics superior to gels formed by self-assembly of previously reported synthetic short peptides. Rheological studies of gels composed of oppositely charged mixed AIP molecules (AIP-1 + 2) revealed superior mechanical stability compared to individual peptide networks (AIP-1 and AIP-2) formed by neutralization of net charges through pH change. Adhesion and elasticity properties of AIP mixed nanofibers and charge neutralized AIP-1, AIP-2 nanofibers were analyzed by high resolution force-distance mapping using atomic force microscopy (AFM). Nanomechanical characterization of self-assembled AIP-1 + 2, AIP-1, and AIP-2 nanofibers also confirmed macroscopic rheology results, and mechanical stability of AIP mixed nanofibers was higher compared to individual AIP-1 and AIP-2 nanofibers self-assembled at acidic and basic pH, respectively. Experimental results were supported with molecular dynamics simulations by considering potential noncovalent interactions between the amino acid residues and possible aggregate forms. In addition, HUVEC cells were cultured on AIP mixed nanofibers at pH 7 and biocompatibility and collagen mimetic scaffold properties of the nanofibrous system were observed. Encapsulation of a zwitterionic dye (rhodamine B) within AIP nanofiber network was accomplished at physiological conditions to demonstrate that this network can be utilized for inclusion of soluble factors as a scaffold for cell culture studies. © 2012 American Chemical Society.
- Research Paper 
Showing items related by title, author, creator and subject.
Self-assembled peptide nanofiber templated one-dimensional gold nanostructures exhibiting resistive switching Acar H.; Genc, R.; Urel, M.; Erkal, T.S.; Dana, A.; Guler, M.O. (2012)An amyloid-like peptide molecule self-assembling into one-dimensional nanofiber structure in ethanol was designed and synthesized with functional groups that can bind to gold ions. The peptide nanofibers were used as ...
Self-Assembled Peptide Nanofiber Templated One-Dimensional Gold Nanostructures Exhibiting Resistive Switching Acar, H.; Genc, R.; Urel, M.; Erkal, T. S.; Dana, A.; Guler, M. O. (ACS Publications, 2012-10-30)An amyloid-like peptide molecule self-assembling into one-dimensional nanofiber structure in ethanol was designed and synthesized with functional groups that can bind to gold ions. The peptide nanofibers were used as ...
Toksöz S.; Guler M.O. (2009)Understanding the mechanisms of molecular self-assembly processes in natural materials is an important step to developing new functional materials with useful properties. Recently, various self-assembled materials have ...