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Tuning of hydrogel stiffness using a two-component peptide system for mammalian cell culture.

ABSTRACT: Self-assembling peptide hydrogels (SAPHs) represent emerging cell cultures systems in several biomedical applications. The advantages of SAPHs are mainly ascribed to the absence of toxic chemical cross-linkers, the presence of ECM-like fibrillar structures and the possibility to produce hydrogels with a large range of different mechanical properties. We will present a two-component peptide system with tuneable mechanical properties, consisting of a small pentapeptide (SFFSF-NH2 , SA5N) that acts as a gelator and a larger 21-mer peptide (SFFSF-GVPGVGVPGVG-SFFSF, SA21) designed as a physical cross-linker. The hydrogels formed by different mixtures of the two peptides are made up mainly of antiparallel β-sheet nanofibers entangling in an intricate network. The effect of the addition of SA21 on the morphology of the hydrogels was investigated by atomic force microscopy and transmission electron microscopy and correlated to the mechanical properties of the hydrogel. Finally, the biocompatibility of the hydrogels using 2D cell cultures was tested. © 2018 The Authors. journal Of Biomedical Materials Research Part A Published By Wiley Periodicals, Inc. J Biomed Mater Res Part A: 107A: 535-544, 2019.

SUBMITTER: Scelsi A

PROVIDER: S-EPMC6587839 | biostudies-other | 2019 Mar

REPOSITORIES: biostudies-other

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Tuning of hydrogel stiffness using a two-component peptide system for mammalian cell culture.

Scelsi Alessandra A Bochicchio Brigida B Smith Andrew A Workman Victoria L VL Castillo Diaz Luis A LA Saiani Alberto A Pepe Antonietta A

Journal of biomedical materials research. Part A 20181119 3

Self-assembling peptide hydrogels (SAPHs) represent emerging cell cultures systems in several biomedical applications. The advantages of SAPHs are mainly ascribed to the absence of toxic chemical cross-linkers, the presence of ECM-like fibrillar structures and the possibility to produce hydrogels with a large range of different mechanical properties. We will present a two-component peptide system with tuneable mechanical properties, consisting of a small pentapeptide (SFFSF-NH<sub>2</sub> , SA5N ...[more]

PMID: 30456777

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Project description:Cellular adaptation relies on the development of proper regulatory schemes for accurate control of gene expression levels in response to environmental cues. Over- or under-expression can lead to diminished cell fitness due to increased costs or insufficient benefits. Positive autoregulation is a common regulatory scheme that controls protein expression levels and gives rise to essential features in diverse signaling systems, yet its roles in cell fitness are less understood. It remains largely unknown how much protein expression is 'appropriate' for optimal cell fitness under specific extracellular conditions and how the dynamic environment shapes the regulatory scheme to reach appropriate expression levels. Here, we investigate the correlation of cell fitness and output response with protein expression levels of the E. coli PhoB/PhoR two-component system (TCS). In response to phosphate (Pi)-depletion, the PhoB/PhoR system activates genes involved in phosphorus assimilation as well as genes encoding themselves, similarly to many other positively autoregulated TCSs. We developed a bacteria competition assay in continuous cultures and discovered that different Pi conditions have conflicting requirements of protein expression levels for optimal cell fitness. Pi-replete conditions favored cells with low levels of PhoB/PhoR while Pi-deplete conditions selected for cells with high levels of PhoB/PhoR. These two levels matched PhoB/PhoR concentrations achieved via positive autoregulation in wild-type cells under Pi-replete and -deplete conditions, respectively. The fitness optimum correlates with the wild-type expression level, above which the phosphorylation output saturates, thus further increase in expression presumably provides no additional benefits. Laboratory evolution experiments further indicate that cells with non-ideal protein levels can evolve toward the optimal levels with diverse mutational strategies. Our results suggest that the natural protein expression levels and feedback regulatory schemes of TCSs are evolved to match the phosphorylation output of the system, which is determined by intrinsic activities of TCS proteins.

Dataset Information

Tuning of hydrogel stiffness using a two-component peptide system for mammalian cell culture.

Publications

Tuning of hydrogel stiffness using a two-component peptide system for mammalian cell culture.

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