Influence of the Thermodynamic and Kinetic Control of Self-Assembly on the Microstructure Evolution of Silk-Elastin-Like Recombinamer Hydrogels.

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Arturo Ibáñez-FonsecaJosé Carlos Rodríguez-Cabello

Abstract

Complex recombinant biomaterials that merge the self-assembling properties of different (poly)peptides provide a powerful tool for the achievement of specific structures, such as hydrogel networks, by tuning the thermodynamics and kinetics of the system through a tailored molecular design. In this work, elastin-like (EL) and silk-like (SL) polypeptides are combined to obtain a silk-elastin-like recombinamer (SELR) with dual self-assembly. First, EL domains force the molecule to undergo a phase transition above a precise temperature, which is driven by entropy and occurs very fast. Then, SL motifs interact through the slow formation of β-sheets, stabilized by H-bonds, creating an energy barrier that opposes phase separation. Both events lead to the development of a dynamic microstructure that evolves over time (until a pore size of 49.9 ± 12.7 µm) and to a delayed hydrogel formation (obtained after 2.6 h). Eventually, the network is arrested due to an increase 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 of the SELR from water, which results in a fixed metastable microarchitecture. These porous hydrogels are preliminarily tested as bi...Continue Reading

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Citations

Jun 2, 2020·Frontiers in Bioengineering and Biotechnology·Arturo Ibáñez-FonsecaJosé Carlos Rodríguez-Cabello
Nov 21, 2020·Small·Constancio González-ObesoJosé Carlos Rodríguez-Cabello
Aug 3, 2021·Frontiers in Bioengineering and Biotechnology·Jose Carlos Rodriguez-CabelloIrene Montequi
Jul 13, 2021·ACS Biomaterials Science & Engineering·Diego López BarreiroCees M J Sagt

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