Fabrication of Thermo-Responsive Molecular Layers from Self-Assembling Elastin-Like Oligopeptides Containing Cell-Binding Domain for Tissue Engineering

Abstract

Novel thermo-responsive elastin-like oligopeptides containing cell-binding epitope (Arg-Gly-Asp-Ser sequence); arginine-glycine-aspartic acid-serine (RGDS)-elastin-like peptides (ELP) and RGDS-deg-ELP; were newly prepared as building blocks of self-assembled molecular layer for artificial extra cellular matrix. A detailed analysis of the conformation of the oligo(ELP)s in water and their self-assembling behavior onto hydrophobic surfaces were performed by using circular dichroism, Fourier transform infrared spectroscopy (FTIR), atomic force microscopy and water contact angle measurements. The experimental results revealed that both oligo(ELP)s self-assembled onto hydrophobic surfaces and formed molecular layers based on their thermo-responsive conformational change from hydrous random coil to dehydrated β-turn structure. Effective cell adhesion and spreading behaviors were observed on these self-assembled oligo(ELP) layers. In addition, attached cells were found to be recovered successfully as a cell-sheet by temperature-induced disassembly of oligo(ELP) layer. This achievement provides an important insight to construct novel oligopeptide-based nano-surfaces for the design of smart artificial extra-cellular matrix. OPEN ACCESSPolymers 2015, 7 135

Modular Self‐Assembling Peptide Platform with a Tunable Thermoresponsiveness via a Single Amino Acid Substitution

“…Atomic force microscopy (AFM) showed that the MELPs coupled with three phenylalanine residues (FFF‐ELPs) self‐assembled into micelle structures (Figure b; Figure S4, Supporting Information). In a temperature‐ramp circular dichroism (CD) study, FFF‐ELPs underwent a gradual coil‐to‐β‐spiral transition similar to the thermal folding behavior of several ELPs in other studies (Figure c) . Based on these results, we determined that the consecutive NAAs can suggest the thermoresponsiveness to MELPs through a phase transition mechanism mediated by micelle self‐assembly.…”

Stimuli-Responsive Block Copolymer-Based Assemblies for Cargo Delivery and Theranostic Applications

“…The LCST of P(HPMA-Lacn) could be tuned in the range of 10–65 °C by varying the grafting density of lactate-containing side chains [ 65 ]. Moreover, ELPs are protein-based materials with the ability to capture drug molecules by undergoing LCST-like phase transition when the polymer solution is heated above its transition temperature [ 68 ]. They are widely used in drug delivery systems owing to their excellent biocompatible and biodegradable properties.…”

Self-Assembly of Short Elastin-like Amphiphilic Peptides: Effects of Temperature, Molecular Hydrophobicity and Charge Distribution

“…Such a phenomenon is usually termed inverse temperature transition (ITT) [13,19,20], which is suggested to be driven by dehydration of the hydrophobic valine side chains [21]. Very interestingly, short elastin-derived peptides with limited number (usually 1–5) of the repeating β-turn units have been shown to have similar temperature-sensitive conformational changes as ELPs [20,21,22,23,24,25,26,27,28,29]. Reiersen et al showed that a single VPGVG unit can act as a thermodynamically independent unit to undergo the temperature-induced extended‒β-turn transition [21].…”