Self-assembly of bacterial amyloid protein nanomaterials on solid surfaces

Önür, Tuğçe; Yuca, Esra; Ölmez, Tolga T.; Şeker, Urartu Özgür Şafak

doi:10.1016/j.jcis.2018.03.016

Cited by 28 publications

(16 citation statements)

References 63 publications

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“…Certain bacteria species, such as Escherichia coli, Mycobacterium tuberculosis, Salmonella typhimurium and Streptomyces coelicolor are able to produce functional amyloids (TerAvest, Li, & Angenent, 2011;Payne et al, 2013). In the literature, some studies have focused on the self-assembly of amyloid proteins obtained from E. coli (Seker, Chen, Citorik, & Lu, 2017;Onur, Yuca, Olmez, & Seker, 2018). For example, Seker et al (2017) developed amyloid curli nanofibers in living communities of E. coli as templates for nanomaterial assembly.…”

Section: Bacterial Proteinsmentioning

confidence: 99%

Self-assembled proteins for food applications: A review

Tomadoni

Capello

Valencia

et al. 2020

Trends in Food Science & Technology

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Section: Bacterial Proteinsmentioning

confidence: 99%

Self-assembled proteins for food applications: A review

Tomadoni

Capello

Valencia

et al. 2020

Trends in Food Science & Technology

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“…We cloned the region encoding the CsgA and CsgB proteins without the signal sequence in our previous study 17 . CsgA and CsgB proteins were expressed and purified as previously described.…”

Section: Purification Of Csga and Csgb Curli Subunitsmentioning

confidence: 99%

“…Ours and other's studies have investigated the use of CsgA and CsgB amyloid subunits for bioinspired materials production and bioinspired processes or device development. In our previous study, we optimized the recombinant production and biochemical properties of CsgA and CsgB curli protein mutants 17 . Controlling the production and secretion of CsgA and CsgB amyloid proteins is critical in terms of final mechanical characteristics of the biofilm-based material assembly.…”

Section: Introductionmentioning

confidence: 99%

Binding Behavior of Microbial Functional Amyloids on Solid Surfaces

Yuca

Kehribar

Şeker

2020

Preprint

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KEYWORDS (Word Style "BG_Keywords"). If you are submitting your paper to a journal that requires keywords, provide significant keywords to aid the reader in literature retrieval. ABSTRACTSelf-assembling protein subunits hold great potential as biomaterials with improved functions.Among the self-assembled protein structures functional amyloids are promising unique properties such as resistance to harsh physical and chemical conditions their mechanical strength, and ease of functionalization. Curli proteins, which are functional amyloids of bacterial biofilms can be programmed as intelligent biomaterials. In order to obtain controllable curli based biomaterials for biomedical applications, and to understand role of each of the curli forming monomeric proteins (namely CsgA and CsgB from Escherichia coli) we characterized their binding kinetics to gold, hydroxyapatite, and silica surfaces. We demonstrated that CsgA, CsgB, and their equimolar mixture have different binding strengths for different surfaces. On hydroxyapatite and silica surfaces, CsgB is the crucial element that determines the final adhesiveness of the CsgA-CsgB mixture. On the gold surface, on the other hand, CsgA controls the behavior of the mixture. Those findings uncover the binding behavior of curli proteins CsgA and CsgB on different biomedically valuable surfaces to obtain a more precise control on their adhesion to a targeted surface.

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“…CsgA and CsgB are the major and minor curli protein subunits, respectively, and they are secreted to the extracellular environment with the help of other curli proteins . Previous studies have accomplished the engineering of the CsgA protein to create biofilms with different functions, such as catalysts, electrical conductors, self‐assembled materials on solid surfaces, and adhesives for underwater applications …”

Section: Introductionmentioning

confidence: 99%

Cellular Biocatalysts Using Synthetic Genetic Circuits for Prolonged and Durable Enzymatic Activity

et al. 2019

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Cellular biocatalysts hold great promise for the synthesis of difficult to achieve compounds, such as complex active molecules. Whole‐cell biocatalysts can be programmed through genetic circuits to be more efficient, but they suffer from low stability. The catalytic activity of whole cells decays under stressful conditions, such as prolonged incubation times or high temperatures. In nature, microbial communities cope with these conditions by forming biofilm structures. In this study, it is shown that the use of biofilm structures can enhance the stability of whole‐cell biocatalysts. We employed two different strategies to increase the stability of whole‐cell catalysts and decrease their susceptibility to high temperature. In the first approach, the formation of a biofilm structure is induced by controlling the expression of one of the curli component, CsgA. The alkaline phosphatase (ALP) enzyme was used to monitor the catalytic activity of cells in the biofilm structure. In the second approach, the ALP enzyme was fused to the CsgA curli fiber subunit to utilize the protective properties of the biofilm on enzyme biofilms. Furthermore, an AND logic gate is introduced between the expression of CsgA and ALP by toehold RNA switches and recombinases to enable logical programming of the whole‐cell catalyst for biofilm formation and catalytic action with different tools. The study presents viable approaches to engineer a platform for biocatalysis processes.

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Self-assembly of bacterial amyloid protein nanomaterials on solid surfaces

Cited by 28 publications

References 63 publications

Self-assembled proteins for food applications: A review

Self-assembled proteins for food applications: A review

Binding Behavior of Microbial Functional Amyloids on Solid Surfaces

Cellular Biocatalysts Using Synthetic Genetic Circuits for Prolonged and Durable Enzymatic Activity

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