RT info:eu-repo/semantics/article
T1 Tuning the stiffness of surfaces by assembling genetically engineered polypeptides with tailored amino acid sequence
A1 Costa, Rui R.
A1 González Pérez, Miguel
A1 Herrero Gutiérrez, Marcos
A1 Pires, Ricardo A.
A1 Alonso Rodrigo, Matilde
A1 Rodríguez Cabello, José Carlos
A1 Reis, Rui Luís
A1 Pashkuleva, Iva
K1 Modificación de superficie
K1 Surface modification
K1 Polipéptidos
K1 Polypeptides
AB We introduce elastin-like recombinamers (ELRs) as polypeptides with precise amino acidpositioning 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 withthe amine-reactive tetrakis (hydroxymethyl) phosphonium chloride compound. We evaluated the affinity, the conformation, and the dissipative behavior of ELRs assembled on alkanethiol selfassembled 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.
PB ACS Publications
SN 1525-7797
YR 2018
FD 2018
LK http://uvadoc.uva.es/handle/10324/35331
UL http://uvadoc.uva.es/handle/10324/35331
LA eng
NO Biomacromolecules, 2018, Vol. 19, n. 8. p. 3401-3411
NO Producción Científica
DS UVaDOC
RD 24-abr-2024