@article {19560,
	title = {Tuning the stiffness of surfaces by assembling genetically engineered polypeptides with tailored amino acid sequence},
	journal = {Biomacromolecules},
	volume = {19},
	year = {2018},
	month = {2018-07-04 00:00:00},
	pages = {3401{\textendash}3411},
	publisher = {ACS},
	abstract = {<p class="p1">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, the conformation, and the dissipative behavior of ELRs assembled on alkanethiol self-assembled coatings by quartz crystal microbalance with dissipation monitoring, multi-parametric surface plasmon resonance, and atomic force microscopy. The thickness of the polypeptide coatings showcase 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.</p>},
	keywords = {Biomaterials, Elastin-like recombinamers, multi-parametric surface plasmon resonance, quartz-crystal microbalance, Surface modification},
	issn = {1525-7797},
	doi = {10.1021/acs.biomac.8b00723},
	url = {https://pubs.acs.org/doi/10.1021/acs.biomac.8b00723},
	author = {Costa, R. R. and Gonz{\'a}lez-P{\'e}rez, M. and Herrero-Guti{\'e}rrez, M. and Pires, R. A. and Alonso, M. and Rodr{\'\i}guez-Cabello, J. C. and Reis, R. L. and Pashkuleva, I.}
}
