Benchmarking of Cph1 Mutants and DrBphP for Light-Responsive Phytochrome-Based Hydrogels with Reversibly Adjustable Mechanical Properties.
Bacterial Proteins
/ chemistry
Benchmarking
Cyanobacteria
/ genetics
Escherichia coli
/ metabolism
Fibroblasts
Genetic Engineering
Humans
Hydrogels
/ chemistry
Mechanotransduction, Cellular
/ radiation effects
Optogenetics
Photoreceptors, Microbial
/ chemistry
Phytochrome
/ chemistry
Protein Kinases
/ chemistry
Viscosity
biomaterials
extracellular matrix
hydrogels
mechanosensing
molecular optogenetics
phytochromes
Journal
Advanced biology
ISSN: 2701-0198
Titre abrégé: Adv Biol (Weinh)
Pays: Germany
ID NLM: 101775319
Informations de publication
Date de publication:
07 2022
07 2022
Historique:
revised:
31
03
2022
received:
30
09
2020
pubmed:
29
4
2022
medline:
19
7
2022
entrez:
28
4
2022
Statut:
ppublish
Résumé
In the rapidly expanding field of molecular optogenetics, the performance of the engineered systems relies on the switching properties of the underlying genetically encoded photoreceptors. In this study, the bacterial phytochromes Cph1 and DrBphP are engineered, recombinantly produced in Escherichia coli, and characterized regarding their switching properties in order to synthesize biohybrid hydrogels with increased light-responsive stiffness modulations. The R472A mutant of the cyanobacterial phytochrome 1 (Cph1) is identified to confer the phytochrome-based hydrogels with an increased dynamic range for the storage modulus but a different light-response for the loss modulus compared to the original Cph1-based hydrogel. Stiffness measurements of human atrial fibroblasts grown on these hydrogels suggest that differences in the loss modulus at comparable changes in the storage modulus affect cell stiffness and thus underline the importance of matrix viscoelasticity on cellular mechanotransduction. The hydrogels presented here are of interest for analyzing how mammalian cells respond to dynamic viscoelastic cues. Moreover, the Cph1-R472A mutant, as well as the benchmarking of the other phytochrome variants, are expected to foster the development and performance of future optogenetic systems.
Identifiants
pubmed: 35481696
doi: 10.1002/adbi.202000337
doi:
Substances chimiques
Bacterial Proteins
0
Hydrogels
0
Photoreceptors, Microbial
0
Phytochrome
11121-56-5
Protein Kinases
EC 2.7.-
Cph1 phytochrome protein, bacteria
EC 2.7.3.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2000337Informations de copyright
© 2022 The Authors. Advanced Biology published by Wiley-VCH GmbH.
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