Modular protein domains: an engineering approach toward functional biomaterials

Lin, Charng‐Yu; Liu, Julie C.

doi:10.1016/j.copbio.2016.02.011

Cited by 44 publications

(33 citation statements)

References 54 publications

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“…This includes modules for cellular adhesion, growth factor activity, mineralization, proteolytic degradation, antimicrobial activity, etc. (DiMarco and Heilshorn, 2012; Liu, 2016).…”

Section: Protein Polymers Produced In P Pastorismentioning

confidence: 99%

Production of protein-based polymers in Pichia pastoris

Werten

Eggink

Stuart

et al. 2019

Biotechnology Advances

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Materials science and genetic engineering have joined forces over the last three decades in the development of so-called protein-based polymers. These are proteins, typically with repetitive amino acid sequences, that have such physical properties that they can be used as functional materials. Well-known natural examples are collagen, silk, and elastin, but also artificial sequences have been devised. These proteins can be produced in a suitable host via recombinant DNA technology, and it is this inherent control over monomer sequence and molecular size that renders this class of polymers of particular interest to the fields of nanomaterials and biomedical research. Traditionally, Escherichia coli has been the main workhorse for the production of these polymers, but the methylotrophic yeast Pichia pastoris is finding increased use in view of the often high yields and potential bioprocessing benefits. We here provide an overview of protein-based polymers produced in P. pastoris . We summarize their physicochemical properties, briefly note possible applications, and detail their biosynthesis. Some challenges that may be faced when using P. pastoris for polymer production are identified: (i) low yields and poor process control in shake flask cultures; i.e. , the need for bioreactors, (ii) proteolytic degradation, and (iii) self-assembly in vivo . Strategies to overcome these challenges are discussed, which we anticipate will be of interest also to readers involved in protein expression in P. pastoris in general.

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“…This includes modules for cellular adhesion, growth factor activity, mineralization, proteolytic degradation, antimicrobial activity, etc. (DiMarco and Heilshorn, 2012; Liu, 2016).…”

Section: Protein Polymers Produced In P Pastorismentioning

confidence: 99%

Production of protein-based polymers in Pichia pastoris

Werten

Eggink

Stuart

et al. 2019

Biotechnology Advances

View full text Add to dashboard Cite

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“…Materials from naturally occurring and recombinant proteins are frequently employed for the study of fundamental biological processes and leveraged for applications in fields as diverse as electronics, optics, bioengineering, medicine, and fashion ( 1 – 13 ). Such broad utility is enabled by the numerous advantageous characteristics of protein-based materials, which include sequence modularity, controllable self-assembly, stimuli-responsiveness, straightforward processability, inherent biological compatibility, and customizable functionality ( 1 – 13 ). Within this context, unique structural proteins known as reflectins have recently attracted substantial attention because of their key roles in the fascinating color-changing capabilities of cephalopods, such as the squid shown in Fig.…”

mentioning

confidence: 99%

Structure, self-assembly, and properties of a truncated reflectin variant

Umerani

Pratakshya

Chatterjee

et al. 2020

Proc. Natl. Acad. Sci. U.S.A.

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Naturally occurring and recombinant protein-based materials are frequently employed for the study of fundamental biological processes and are often leveraged for applications in areas as diverse as electronics, optics, bioengineering, medicine, and even fashion. Within this context, unique structural proteins known as reflectins have recently attracted substantial attention due to their key roles in the fascinating color-changing capabilities of cephalopods and their technological potential as biophotonic and bioelectronic materials. However, progress toward understanding reflectins has been hindered by their atypical aromatic and charged residue-enriched sequences, extreme sensitivities to subtle changes in environmental conditions, and well-known propensities for aggregation. Herein, we elucidate the structure of a reflectin variant at the molecular level, demonstrate a straightforward mechanical agitation-based methodology for controlling this variant’s hierarchical assembly, and establish a direct correlation between the protein’s structural characteristics and intrinsic optical properties. Altogether, our findings address multiple challenges associated with the development of reflectins as materials, furnish molecular-level insight into the mechanistic underpinnings of cephalopod skin cells’ color-changing functionalities, and may inform new research directions across biochemistry, cellular biology, bioengineering, and optics.

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“…In parallel with what was discussed for peptide-based hydrogels in Section 2.2.1, protein-based hydrogels are gaining interest in literature. Although catalysis is generally not the main topic [32], a few interesting examples of catalytic protein-hydrogels were reported in literature quite recently [33][34][35]. In these systems crosslinking was noncovalent and achieved via oligomerization of specific protein domains, such as the trimeric CutA protein [33,34] or homodimeric phosphite dehydrogenase (PTDH) [35].…”

Section: Protein-based Catalytic Hydrogelsmentioning

confidence: 99%