Bacterial Amyloids: Biogenesis and Biomaterials

Publikation: Bidrag til bog/antologi/rapport/proceedingBidrag til bog/antologiForskningpeer review

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Bacterial Amyloids : Biogenesis and Biomaterials. / Christensen, Line Friis Bakmann; Schafer, Nicholas; Wolf-Perez, Adriana; Madsen, Daniel Jhaf; Otzen, Daniel E.

Biological and Bio-inspired Nanomaterials. red. / Sarah Perrett; Alexander K. Buell; Tuomas P.J. Knowles. Springer, 2019. s. 113-159 (Advances in Experimental Medicine and Biology, Bind 1174).

Publikation: Bidrag til bog/antologi/rapport/proceedingBidrag til bog/antologiForskningpeer review

Harvard

Christensen, LFB, Schafer, N, Wolf-Perez, A, Madsen, DJ & Otzen, DE 2019, Bacterial Amyloids: Biogenesis and Biomaterials. i S Perrett, AK Buell & TPJ Knowles (red), Biological and Bio-inspired Nanomaterials. Springer, Advances in Experimental Medicine and Biology, bind 1174, s. 113-159. https://doi.org/10.1007/978-981-13-9791-2_4

APA

Christensen, L. F. B., Schafer, N., Wolf-Perez, A., Madsen, D. J., & Otzen, D. E. (2019). Bacterial Amyloids: Biogenesis and Biomaterials. I S. Perrett, A. K. Buell, & T. P. J. Knowles (red.), Biological and Bio-inspired Nanomaterials (s. 113-159). Springer. Advances in Experimental Medicine and Biology, Bind. 1174 https://doi.org/10.1007/978-981-13-9791-2_4

CBE

Christensen LFB, Schafer N, Wolf-Perez A, Madsen DJ, Otzen DE. 2019. Bacterial Amyloids: Biogenesis and Biomaterials. Perrett S, Buell AK, Knowles TPJ, red. I Biological and Bio-inspired Nanomaterials. Springer. s. 113-159. (Advances in Experimental Medicine and Biology, Bind 1174). https://doi.org/10.1007/978-981-13-9791-2_4

MLA

Christensen, Line Friis Bakmann o.a.. "Bacterial Amyloids: Biogenesis and Biomaterials"., Perrett, Sarah Buell, Alexander K. Knowles, Tuomas P.J. (red.). Biological and Bio-inspired Nanomaterials. Springer. (Advances in Experimental Medicine and Biology, Bind 1174). 2019, 113-159. https://doi.org/10.1007/978-981-13-9791-2_4

Vancouver

Christensen LFB, Schafer N, Wolf-Perez A, Madsen DJ, Otzen DE. Bacterial Amyloids: Biogenesis and Biomaterials. I Perrett S, Buell AK, Knowles TPJ, red., Biological and Bio-inspired Nanomaterials. Springer. 2019. s. 113-159. (Advances in Experimental Medicine and Biology, Bind 1174). https://doi.org/10.1007/978-981-13-9791-2_4

Author

Christensen, Line Friis Bakmann ; Schafer, Nicholas ; Wolf-Perez, Adriana ; Madsen, Daniel Jhaf ; Otzen, Daniel E. / Bacterial Amyloids : Biogenesis and Biomaterials. Biological and Bio-inspired Nanomaterials. red. / Sarah Perrett ; Alexander K. Buell ; Tuomas P.J. Knowles. Springer, 2019. s. 113-159 (Advances in Experimental Medicine and Biology, Bind 1174).

Bibtex

@inbook{3934e56120234837bc027f06253b02fc,
title = "Bacterial Amyloids: Biogenesis and Biomaterials",
abstract = "Functional amyloid (FuBA) is produced by a large fraction of all bacterial species and represents a constructive use of the stable amyloid fold, in contrast to the pathological amyloid seen in neurodegenerative diseases. When assembled into amyloid, FuBA is unusually robust and withstands most chemicals including denaturants and SDS. Uses include strengthening of bacterial biofilms, cell-to-cell communication, cell wall construction and even bacterial warfare. Biogenesis is under tight spatio-temporal control, thanks to a simple but efficient secretion system which in E. coli, Pseudomonas and other well-studied bacteria includes a major amyloid component that is kept unfolded in the periplasm thanks to chaperones, threaded through the outer membrane via a pore protein and anchored to the cell surface through a nucleator and possibly other helper proteins. In these systems, amyloid formation is promoted through imperfect repeats, but other evolutionarily unrelated proteins either have no or only partially conserved repeats or simply consist of small peptides with multiple structural roles. This makes bioinformatics analysis challenging, though the sophisticated amyloid prediction tools developed from research in pathological amyloid together with the steady increase in identification of further examples of amyloid will strengthen genomic data mining. Functional amyloid represents an intriguing source of robust yet biodegradable materials with new properties, when combining the optimized self-assembly properties of the amyloid component with e.g. peptides with different binding properties or surface-reactive protein binders. Sophisticated patterns can also be obtained by co-incubating bacteria producing different types of amyloid, while amyloid inclusion bodies may lead to slow-release nanopills.",
author = "Christensen, {Line Friis Bakmann} and Nicholas Schafer and Adriana Wolf-Perez and Madsen, {Daniel Jhaf} and Otzen, {Daniel E}",
year = "2019",
doi = "10.1007/978-981-13-9791-2_4",
language = "English",
isbn = "978-981-13-9790-5",
series = "Advances in Experimental Medicine and Biology",
publisher = "Springer",
pages = "113--159",
editor = "Sarah Perrett and Buell, {Alexander K.} and Knowles, {Tuomas P.J.}",
booktitle = "Biological and Bio-inspired Nanomaterials",

}

RIS

TY - CHAP

T1 - Bacterial Amyloids

T2 - Biogenesis and Biomaterials

AU - Christensen, Line Friis Bakmann

AU - Schafer, Nicholas

AU - Wolf-Perez, Adriana

AU - Madsen, Daniel Jhaf

AU - Otzen, Daniel E

PY - 2019

Y1 - 2019

N2 - Functional amyloid (FuBA) is produced by a large fraction of all bacterial species and represents a constructive use of the stable amyloid fold, in contrast to the pathological amyloid seen in neurodegenerative diseases. When assembled into amyloid, FuBA is unusually robust and withstands most chemicals including denaturants and SDS. Uses include strengthening of bacterial biofilms, cell-to-cell communication, cell wall construction and even bacterial warfare. Biogenesis is under tight spatio-temporal control, thanks to a simple but efficient secretion system which in E. coli, Pseudomonas and other well-studied bacteria includes a major amyloid component that is kept unfolded in the periplasm thanks to chaperones, threaded through the outer membrane via a pore protein and anchored to the cell surface through a nucleator and possibly other helper proteins. In these systems, amyloid formation is promoted through imperfect repeats, but other evolutionarily unrelated proteins either have no or only partially conserved repeats or simply consist of small peptides with multiple structural roles. This makes bioinformatics analysis challenging, though the sophisticated amyloid prediction tools developed from research in pathological amyloid together with the steady increase in identification of further examples of amyloid will strengthen genomic data mining. Functional amyloid represents an intriguing source of robust yet biodegradable materials with new properties, when combining the optimized self-assembly properties of the amyloid component with e.g. peptides with different binding properties or surface-reactive protein binders. Sophisticated patterns can also be obtained by co-incubating bacteria producing different types of amyloid, while amyloid inclusion bodies may lead to slow-release nanopills.

AB - Functional amyloid (FuBA) is produced by a large fraction of all bacterial species and represents a constructive use of the stable amyloid fold, in contrast to the pathological amyloid seen in neurodegenerative diseases. When assembled into amyloid, FuBA is unusually robust and withstands most chemicals including denaturants and SDS. Uses include strengthening of bacterial biofilms, cell-to-cell communication, cell wall construction and even bacterial warfare. Biogenesis is under tight spatio-temporal control, thanks to a simple but efficient secretion system which in E. coli, Pseudomonas and other well-studied bacteria includes a major amyloid component that is kept unfolded in the periplasm thanks to chaperones, threaded through the outer membrane via a pore protein and anchored to the cell surface through a nucleator and possibly other helper proteins. In these systems, amyloid formation is promoted through imperfect repeats, but other evolutionarily unrelated proteins either have no or only partially conserved repeats or simply consist of small peptides with multiple structural roles. This makes bioinformatics analysis challenging, though the sophisticated amyloid prediction tools developed from research in pathological amyloid together with the steady increase in identification of further examples of amyloid will strengthen genomic data mining. Functional amyloid represents an intriguing source of robust yet biodegradable materials with new properties, when combining the optimized self-assembly properties of the amyloid component with e.g. peptides with different binding properties or surface-reactive protein binders. Sophisticated patterns can also be obtained by co-incubating bacteria producing different types of amyloid, while amyloid inclusion bodies may lead to slow-release nanopills.

U2 - 10.1007/978-981-13-9791-2_4

DO - 10.1007/978-981-13-9791-2_4

M3 - Book chapter

C2 - 31713198

SN - 978-981-13-9790-5

T3 - Advances in Experimental Medicine and Biology

SP - 113

EP - 159

BT - Biological and Bio-inspired Nanomaterials

A2 - Perrett, Sarah

A2 - Buell, Alexander K.

A2 - Knowles, Tuomas P.J.

PB - Springer

ER -