Tuning the Stiffness of Surfaces by Assembling Genetically Engineered Polypeptides with Tailored Amino Acid Sequence

Publication year: 2018
Authors: Costa R.R. 1,2, González-Pérez M. 3,4, Herrero-Gutiérrez M. 3,4, Pires R.A. 1,2,5, Alonso M. 3,4, Rodriguez-Cabello J.C. 3,4, Reis R.L. 1,2,5, Pashkuleva I. 1,2
Affiliations:

1 - 3B's Research Group, I3Bs-Research Institute on Biomaterials, Biodegradables and Biomimetics, University of Minho, Headquarters of the European Institute of Excellence on Tissue Engineering and Regenerative Medicine, AvePark, Parque de Ciência e Tecnologia, Zona Industrial da Gandra, 4805-017 Barco, Guimarães , Portugal
2 - ICVS/3B's, PT Government Associated Laboratory, Braga/Guimarães, Portugal
3 - G.I.R. Bioforge, University of Valladolid, CIBER-BBN, Edificio LUCIA, Paseo de Belén, 19, 47011 Valladolid, Spain
4 - Networking Research Center on Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN) Valladolid, Spain
5 - The Discoveries Centre for Regenerative and Precision Medicine, Headquarters at University of Minho, Avepark, 4805-017 Barco, Guimarães, Portugal

Published in: Biomacromolecules, 2018, Vol. 19(8), p. 3401-3411
doi: 10.1021/acs.biomac.8b00723

We introduce elastin-like recombinamers (ELRs) as polypeptides with precise amino acid positioning to generate polypeptide coatings with tunable rigidity. Two ELRs are used: V84-ELR, a hydrophobic monoblock, and EI-ELR, an amphiphilic diblock. Both were modified with the amine-reactive tetrakis (hydroxymethyl) phosphonium chloride compound. We evaluated the affinity, conformation, and dissipative behavior of ELRs assembled on alkanethiol self-assembled coatings by quartz crystal microbalance with dissipation monitoring, multiparametric surface plasmon resonance, and atomic force microscopy. The thickness of the polypeptide coatings showcases the preferential affinity of ELRs to NH2- and CH3-terminated surfaces. We demonstrate that V84-ELR strongly bonded to the substrate and reorganizes into an extended and more hydrated layer as the adsorbed amount increases, whereas EI-ELR has a less dissipative behavior. The results suggest that ELR adsorption depends on the amino acid sequence and the substrate chemistry, ultimately influencing the stiffness of the polypeptide coatings.


MP-SPR keywords: alkanethiol SAMs, bound mass, elastin-like recombinamers (ELRs) as polypeptides, hydration, interaction, layer thickness, refractive index, self-assembly monolayer