RT info:eu-repo/semantics/article
T1 Influence of the Thermodynamic and Kinetic Control of Self‐Assembly on the Microstructure Evolution of Silk‐Elastin‐Like Recombinamer Hydrogels
A1 Ibáñez Fonseca, Arturo
A1 Orbanic, Doriana
A1 Arias Vallejo, Francisco Javier
A1 Alonso Rodrigo, Matilde
A1 Zeugolis, Dimitrios I.
A1 Rodríguez Cabello, José Carlos
AB Complex recombinant biomaterials that merge the self-assemblingproperties of different (poly)peptides provide a powerful tool for theachievement of specific structures, such as hydrogel networks, by tuningthe thermodynamics and kinetics of the system through a tailored moleculardesign. In this work, elastin-like (EL) and silk-like (SL) polypeptides arecombined to obtain a silk-elastin-like recombinamer (SELR) with dual selfassembly. First, EL domains force the molecule to undergo a phase transitionabove a precise temperature, which is driven by entropy and occurs very fast.Then, SL motifs interact through the slow formation of β-sheets, stabilizedby H-bonds, creating an energy barrier that opposes phase separation. Bothevents lead to the development of a dynamic microstructure that evolvesover time (until a pore size of 49.9 ± 12.7 µm) and to a delayed hydrogelformation (obtained after 2.6 h). Eventually, the network is arrested due to anincrease in β-sheet secondary structures (up to 71.8 ± 0.8%) within SL motifs.This gives a high bond strength that prevents the complete segregation ofthe SELR from water, which results in a fixed metastable microarchitecture.These porous hydrogels are preliminarily tested as biomimetic niches for theisolation of cells in 3D cultures.
PB WILEY-VCH
SN 1613-6810
YR 2020
FD 2020
LK http://uvadoc.uva.es/handle/10324/42387
UL http://uvadoc.uva.es/handle/10324/42387
LA spa
NO Small, junio 2020, vol 16, p. 2001244
DS UVaDOC
RD 24-abr-2024