Microbial production of megadalton titin yields fibers with advantageous mechanical properties

Bowen, C. Vaughan A.; Sargent, Cameron J.; Wang, Ao; Zhu, Yaguang; Chang, Xinyuan; Li, Jingyao; Mu, Xinyue; Galazka, Jonathan M.; Jun, Young‐Shin; Keten, Sinan; Zhang, Fuzhong

doi:10.1038/s41467-021-25360-6

Cited by 31 publications

(34 citation statements)

References 80 publications

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“…There are also studies about characterizing individual proteins of interest: Bowen et al. ( 35 ) microbially produced high-performance titin polymers and used CD to examine the secondary structure and fold of the purified polymers. Balacescu et al.…”

Section: Resultsmentioning

confidence: 99%

BeStSel: webserver for secondary structure and fold prediction for protein CD spectroscopy

Micsonai

Moussong

Wien

et al. 2022

Nucleic Acids Research

207

121

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Circular dichroism (CD) spectroscopy is widely used to characterize the secondary structure composition of proteins. To derive accurate and detailed structural information from the CD spectra, we have developed the Beta Structure Selection (BeStSel) method (PNAS, 112, E3095), which can handle the spectral diversity of β-structured proteins. The BeStSel webserver provides this method with useful accessories to the community with the main goal to analyze single or multiple protein CD spectra. Uniquely, BeStSel provides information on eight secondary structure components including parallel β-structure and antiparallel β-sheets with three different groups of twist. It overperforms any available method in accuracy and information content, moreover, it is capable of predicting the protein fold down to the topology/homology level of the CATH classification. A new module of the webserver helps to distinguish intrinsically disordered proteins by their CD spectrum. Secondary structure calculation for uploaded PDB files will help the experimental verification of protein MD and in silico modelling using CD spectroscopy. The server also calculates extinction coefficients from the primary sequence for CD users to determine the accurate protein concentrations which is a prerequisite for reliable secondary structure determination. The BeStSel server can be freely accessed at https://bestsel.elte.hu.

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Section: Resultsmentioning

confidence: 99%

BeStSel: webserver for secondary structure and fold prediction for protein CD spectroscopy

Micsonai

Moussong

Wien

et al. 2022

Nucleic Acids Research

207

121

View full text Add to dashboard Cite

show abstract

“…We fused split Mfp5 fragments to three types of fiber proteins, including a recombinant spider silk 16xAAA (polyalanine) 9 , another amyloid-silk hybrid protein 16xKLV 10 , and a titin fragment Ig67-70 11 . These fiber materials use different molecular interaction mechanisms and form different sizes and portion of β-nanocrystals 10 , 11 . Bi-terminal fusion of split Mfp5 fragments enhanced fiber ultimate tensile strength by 65.5-139% for all three proteins (Fig.…”

Section: Resultsmentioning

confidence: 99%

Bi-terminal fusion of intrinsically-disordered mussel foot protein fragments boosts mechanical strength for protein fibers

Jiang

Chang

et al. 2023

Nat Commun

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Microbially-synthesized protein-based materials are attractive replacements for petroleum-derived synthetic polymers. However, the high molecular weight, high repetitiveness, and highly-biased amino acid composition of high-performance protein-based materials have restricted their production and widespread use. Here we present a general strategy for enhancing both strength and toughness of low-molecular-weight protein-based materials by fusing intrinsically-disordered mussel foot protein fragments to their termini, thereby promoting end-to-end protein-protein interactions. We demonstrate that fibers of a ~60 kDa bi-terminally fused amyloid-silk protein exhibit ultimate tensile strength up to 481 ± 31 MPa and toughness of 179 ± 39 MJ*m−3, while achieving a high titer of 8.0 ± 0.70 g/L by bioreactor production. We show that bi-terminal fusion of Mfp5 fragments significantly enhances the alignment of β-nanocrystals, and intermolecular interactions are promoted by cation-π and π-π interactions between terminal fragments. Our approach highlights the advantage of self-interacting intrinsically-disordered proteins in enhancing material mechanical properties and can be applied to a wide range of protein-based materials.

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“…These ECMs present a unique pattern combined with the isotropic and anisotropic surface. [55,59,71] Thus, it is inevitably necessary to fabricate a tissue-mimicking biomaterial to investigate the cell response to a dynamic surface change. This study found that the cells' aspect ratio and spreading area on the BMAF surfaces increased progressively with the BMAF orientation degree.…”

Section: Bmaf-induced Cell Cytoskeleton Reorganizationmentioning

confidence: 99%

Natural Silk Spinning‐Inspired Meso‐Assembly‐Processing Engineering Strategy for Fabricating Soft Tissue‐Mimicking Biomaterials

Zhang

Cao

et al. 2022

Adv Funct Materials

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Natural silk spinning is the strategy used by spiders and silkworms to construct their ultra-strong-and-tough silks. It can be considered as an optimized meso-assembly processing engineering (MAPE) strategy that effectively coordinates molecular-and-supramolecular assembly and native spinning. Inspired by this process, this study develops a biomimetic MAPE strategy to fabricate biomaterials mimicking the structural and mechanical characteristics of biological tissues. The structural and mechanical mimetics are realized by synergistically integrating phase transition-induced meso-assembly and mechanical training-induced structural remodeling. Through this approach, highly-hydrated silk fibroin materials with exceptional tunable mechanical properties, such as softness, high stretchability (failure strain larger than 1200%), and high strength and toughness (strength of 5 ± 1 MPa, stiffness 18 ± 2 MPa, and toughness of 6 ± 1 MJ m −3 ) are produced. Thanks to their structural and mechanical tissue-matching features, these biomimetic mesoassembled materials exhibit advances in the modulation of different cell morphologies. The gradient architecture deformation (aspect ratio, spreading area, and perimeter) is evidenced, and the interplay between cytoskeleton (actin and tubulin) and matrix adaptation orientation is substantiated. These findings advance the application of silk fibroin biomaterials in the regulation of adaptive cell reconstruction, since the morphology of cells is the basis for their physiological functions.

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Microbial production of megadalton titin yields fibers with advantageous mechanical properties

Cited by 31 publications

References 80 publications

BeStSel: webserver for secondary structure and fold prediction for protein CD spectroscopy

BeStSel: webserver for secondary structure and fold prediction for protein CD spectroscopy

Bi-terminal fusion of intrinsically-disordered mussel foot protein fragments boosts mechanical strength for protein fibers

Natural Silk Spinning‐Inspired Meso‐Assembly‐Processing Engineering Strategy for Fabricating Soft Tissue‐Mimicking Biomaterials

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