Investigation of Self-assembly Structure and Properties of a Novel Designed Lego-type Peptide with Double Amphiphilic Surfaces

Abstract

A typically designed 'Peptide Lego' has two distinct surfaces: a hydrophilic side that contains the complete charge distribution and a hydrophobic side. In this article, we describe the fabrication of a unique lego-type peptide with the AEAEYAKAK sequence. The novel peptide with double amphiphilic surfaces is different from typical peptides due to special arrangement of the residues. The results of CD, FT-IR, AFM and DLS demonstrate that the peptide with the random coil characteristic was able to form stable nanostructures that were mediated by non-covalent interactions in an aqueous solution. The data further indicated that despite its different structure, the peptide was able to undergo self-assembly similar to a typical peptide. In addition, the use of hydrophobic pyrene as a model allowed the peptide to provide a new type of potential nanomaterial for drug delivery. These efforts collectively open up a new direction in the fabrication of nanomaterials that are more perfect and versatile.

Characterization of Fiber-Forming Peptides and Proteins by Means of Atomic Force Microscopy

“…An aqueous solution KLD-12 was used for injection into a mesenchymal stem cell culture, where the physiologically relevant ionic strength of the cell media caused the formation of the gel, encapsulating stem cells to create a 3D scaffold. Wang et al [218] formed fibers from random coil peptides based on an alanine, glutamic acid, tyrosine and lysinebased sequence (AEAEYAKAK), which formed dense, directional fibers ( Figure 17) formed by a 'Lego-type assembly'. No characteristic ordered secondary structure motif was identified in the assembled fibers.…”