Spontaneous Alignment of Self‐Assembled Cationic and Amphiphilic β‐Sheet Peptides

• Published in: Advanced materials interfaces Vol. 7; no. 14
• Main Authors: Yosefi, Gal, Cohen‐Erez, Ifat, Nativ‐Roth, Einat, Rapaport, Hanna, Bitton, Ronit
• Format: Journal Article
• Language: English
• Published: Weinheim John Wiley & Sons, Inc 01-07-2020
• Subjects: Alignment; amphiphilic peptides; anisotropy; Aqueous solutions; Biomedical materials; Cations; Gels; Hydrophobicity; Peptides; Phase transitions; self‐assembly; Shearing; small‐angle X‐ray scattering
• ISSN: 2196-7350; 2196-7350
• DOI: 10.1002/admi.202000332

Aligned peptide assemblies are of interest for both fundamental understanding of biological systems as well as development of novel biomaterials. Herein, Pro‐Lys‐(Phe‐Lys)5‐Pro (PFK), a cationic and amphiphilic β‐sheet synthetic peptide that self‐assembles into fibrils, capable of undergoing spontaneous isotropic to nematic phase transition, that intrinsically aligns in solution, is presented. Upon dissolution PFK forms isotropically dispersed fibrils due to delicate balance between attractive H bonds and hydrophobic interactions to electrostatic repulsive forces. The transition from isotropic to nematic phase alignment occurring over a period of several days is monitored in situ by both small‐angle X‐ray scattering and cryogenic transmission electron microscopy. The degree of alignment and the time required to achieve a complete isotropic–nematic phase transition of PFK fibrils in aqueous solution is found to be concentration dependent as predicted by Onsager's excluded volume theory. Remarkably, PFK nematic phases remain aligned over the course of several months without the application of any external stimuli. Aligned PFK gels can be formed by mild shearing through a salty medium. This system provides a novel route for producing nanoscale aligned materials for potential biomedical applications.
Alignment over different scales has been shown to be an essential feature for the regulation of structure and functionality in biology. This work presents a cationic and amphiphilic β‐sheet synthetic peptide that self‐assembles into fibrils, capable of undergoing spontaneous alignment in solution, without any external stimuli. Using this approach enables the preparation of sophisticated aligned materials for biomedical applications.