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Programmable Self-Assembling Protein Nanomaterials: Current Status and Prospects

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Abstract

Protein-based nanomaterials are increasingly engineered as platforms for applications in biomanufacturing, for biomedical purposes, and as structural and organizational components of new types of living materials. Advances in synthetic biology and computational protein design offer tremendous opportunities for the engineering of new types of protein building blocks that self-assemble autonomously into customizable materials with various morphologies and properties. As proteins are genetically encoded, material production is genetically programmable and can be achieved sustainably with microbial cell factories, or in the future, by using cell-free technologies. An overview will be provided of the different types of self-assembling protein materials currently designed, characterized, and functionalized for a range of applications. Finally, opportunities and challenges for the design of genetically programmable materials that self-organize into new types of hierarchical protein materials with emergent functions will be discussed.

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Abbreviations

1D:

one-dimensional

2D:

two-dimensional

3D:

three-dimensional

ACP:

atmospheric cold plasma

ADH:

alcohol dehydrogenase

AF4:

asymmetric flow field-flow fractionation

AFM:

atomic force microscopy

AI:

aggregation index

AmDH:

amine dehydrogenase

AMP:

antimicrobial peptide

AP:

alkaline phosphatase

Bfr:

Escherichia coli bacterioferritin

BMC:

bacterial microcompartment

CBD:

chitin binding domain

CCMV:

cowpea chlorotic mottle virus

CD:

circular dichroism

CP:

bacteriophage P22 coat protein

Cp149:

hepatitis B virus

CR:

Congo red

Cryo-EM:

cryo-electron microscopy

DCS:

differential centrifugal sedimentation

DLS :

dynamic light scattering

DOX:

doxorubicin

Dps:

DNA-binding protein from starved cells

DSC:

differential scanning calorimeter

DyP:

dye-decolorizing peroxidase

E. coli :

Escherichia coli

EDTA:

ethylenediaminetetraacetic acid

ELP:

elastin-like polypeptide

ELS:

electrophoretic light scattering

ESEM:

environmental scanning electron microscopy

Eut:

ethanolamine utilization

FRET:

Förster resonance energy transfer

GBS:

group B Streptococcus

GBS-NN:

group B Streptococcus antigen

GFP+36:

green fluorescence protein with a charge of +36

GFP:

green fluorescent protein

GOX:

glucose oxidase

GuHCl:

guanidine hydrochloride

HDFM:

hyperspectral dark-field microscopy

HG12:

histidine-rich amphiphile

HRP:

horseradish peroxidase

HuHF:

human H ferritin

IMAC:

immobilized metal affinity chromatography

LS:

lumazine synthase

Mfp:

mussel foot protein

MnP:

manganese peroxidase

MRI:

magnetic resonance imaging

Mx:

Myxococcus xanthus

ncAA:

noncanonical amino acid

NTA:

nanoparticle tracking analysis

PAGE:

polyacrylamide gel electrophoresis

PDC:

pyruvate decarboxylase

PdR:

putidaredoxin reductase

PdX:

putidaredoxin

PEG:

poly(ethylene glycol)

PTM:

posttranslational modification

Qt:

Quasibacillus thermotolerans

RP-HPLC:

reverse phase high performance liquid chromatography

SAXS:

small angle X-ray scattering

SbpA:

Lysinibacillus sphaericus S-layer protein

SEC:

size exclusion chromatography

SEM:

scanning electron microscopy

S-layer:

surface layer

SP:

bacteriophage P22 scaffolding protein

SRCD:

synchrotron radiation circular dichroism

SrtA:

Staphylococcus aureus sortase

TCEP:

tris(2-carboxyethyl) phosphine

TEM:

transmission electron microscopy

TMV:

tobacco mosaic virus

TRPS:

tunable resistive pulse sensing

UAA:

unnatural amino acid

UV-Vis:

ultraviolet-visible light

VLP:

viruslike particle

γ-PFD:

gamma-prefoldin

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Acknowledgments

Research on the development of self-assembling protein materials in the Schmidt-Dannert Laboratory has been supported by Defense Threat Reduction Agency Grant HDTRA-15-0004, Defense Advanced Research Projects Agency Contract HR0011-17-0038, National Science Foundation CBET-1916030, MnDRIVE, and the University of Minnesota’s Biocatalysis Initiative through the BioTechnology Institute. Kelly Wallin was supported by a predoctoral NIH training grant fellowship (5T32 GM008347) and by an NSF graduate research fellowship (CON-75851, Project 00074041).

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KKW, RZ, and CSD wrote this paper.

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The authors declare no conflict of interest.

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  1. Kelly Wallin and Ruijie Zhang contributed equally with all other contributors.

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  1. Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, St. Paul, MN, USA

    Kelly Wallin, Ruijie Zhang & Claudia Schmidt-Dannert

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Correspondence to Claudia Schmidt-Dannert .

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  1. Department of Civil, Environmental, and Architectural Engineering, Materials Science and Engineering Program, University of Colorado Boulder, Boulder, CO, USA

    Wil V. Srubar III

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Wallin, K., Zhang, R., Schmidt-Dannert, C. (2022). Programmable Self-Assembling Protein Nanomaterials: Current Status and Prospects. In: Srubar III, W.V. (eds) Engineered Living Materials. Springer, Cham. https://doi.org/10.1007/978-3-030-92949-7_3

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