Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

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

Ibáñez-Fonseca, Arturo LU orcid ; Orbanic, Doriana LU ; Arias, Francisco Javier ; Alonso, Matilde ; Zeugolis, Dimitrios I and Rodríguez-Cabello, José Carlos (2020) In Small 16(28). p.1-8
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... (More)

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 biomimetic niches for the isolation of cells in 3D cultures.

(Less)
Please use this url to cite or link to this publication:
author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
keywords
Elastin, Hydrogels, Kinetics, Silk, Thermodynamics
in
Small
volume
16
issue
28
article number
e2001244
pages
1 - 8
publisher
John Wiley & Sons Inc.
external identifiers
  • scopus:85085469162
  • pmid:32519515
ISSN
1613-6829
DOI
10.1002/smll.202001244
language
English
LU publication?
yes
additional info
© 2020 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
id
d56cada4-e210-424a-b999-c4268a2376dd
date added to LUP
2025-09-14 19:46:27
date last changed
2025-09-16 03:30:45
@article{d56cada4-e210-424a-b999-c4268a2376dd,
  abstract     = {{<p>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 biomimetic niches for the isolation of cells in 3D cultures.</p>}},
  author       = {{Ibáñez-Fonseca, Arturo and Orbanic, Doriana and Arias, Francisco Javier and Alonso, Matilde and Zeugolis, Dimitrios I and Rodríguez-Cabello, José Carlos}},
  issn         = {{1613-6829}},
  keywords     = {{Elastin; Hydrogels; Kinetics; Silk; Thermodynamics}},
  language     = {{eng}},
  number       = {{28}},
  pages        = {{1--8}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{Small}},
  title        = {{Influence of the Thermodynamic and Kinetic Control of Self-Assembly on the Microstructure Evolution of Silk-Elastin-Like Recombinamer Hydrogels}},
  url          = {{http://dx.doi.org/10.1002/smll.202001244}},
  doi          = {{10.1002/smll.202001244}},
  volume       = {{16}},
  year         = {{2020}},
}