Genetically Engineered Peptides for Inorganics: Study of an Unconstrained Bacterial Display Technology and Bulk Aluminum Alloy

Adams, Bryn L.; Finch, Amethist S.; Hurley, Margaret M.; Sarkes, Deborah A.; Stratis‐Cullum, Dimitra N.

doi:10.1002/adma.201301646

Cited by 23 publications

(40 citation statements)

References 45 publications

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“…62,63 The eCPX peptide library has been used previously for biopanning of affinity peptides to several toxins (Protective Antigen component of Anthrax toxin, 64,65 Staphylococcal Enterotoxin B (SEB) 66 ), as well as GEPI for a bulk aluminum alloy. 23 This scaffold has also been successfully used to display functional peptides developed from phage and allowed for the first direct performance comparison of peptides originating from different scaffolds. 23 It was also used to demonstrate the selectivity of an aluminum alloybinding peptide developed from the eCPX library, for its target alloy over glass, copper or brass.…”

Section: Surface Display Scaffoldsmentioning

confidence: 99%

“…23 This scaffold has also been successfully used to display functional peptides developed from phage and allowed for the first direct performance comparison of peptides originating from different scaffolds. 23 It was also used to demonstrate the selectivity of an aluminum alloybinding peptide developed from the eCPX library, for its target alloy over glass, copper or brass. 67 Regardless of the peptide display library type or host organisms, the key advantage to all biocombinatorial approaches is that the peptide's identity is encoded by the organism's genetic material.…”

Section: Surface Display Scaffoldsmentioning

confidence: 99%

“…Goldbinding peptides are examples of genetically engineered peptides for inorganics (GEPI), and a number of gold-binding peptides have been developed for a variety of applications. A wide range of inorganic materials, including metals, metal oxides, semiconductors, polymers, carbon nanotubes and other functional materials (hydroxylapatite, mica, graphite) [17][18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34][35] have been the focus of previous studies using GEPI. Traditionally, in such studies, emphasis has been focused on peptide binders with the highest affinity for their target.…”

Section: Gold-binding Peptidesmentioning

confidence: 99%

“…Previous combined experimental/molecular dynamics studies of peptide binding on metal and metal oxide systems demonstrated the important role that solvated peptide conformation plays in the binding process. 23,26 Clearly, the large number of factors involved in peptide-surface interactions make this a difficult problem to unravel, both experimentally and computationally.…”

Section: Gold-binding Peptidesmentioning

confidence: 99%

“…These are commonly hosted on Escherichia coli (E. coli), with the peptide library located on a modified flagella (FliTrx) 61 or modified outer membrane protein (eCPX). 23 The eCPX scaffold was the bacterial surface display scaffold used in these studies, and is a circularly permuted form of the OmpX protein that has been optimized to display unconstrained 15mer peptides in E. coli. 62,63 The eCPX peptide library has been used previously for biopanning of affinity peptides to several toxins (Protective Antigen component of Anthrax toxin, 64,65 Staphylococcal Enterotoxin B (SEB) 66 ), as well as GEPI for a bulk aluminum alloy.…”

Section: Surface Display Scaffoldsmentioning

confidence: 99%

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Functional and Selective Bacterial Interfaces Using Cross-Scaffold Gold Binding Peptides

Adams

Hurley

Jahnke

et al. 2015

JOM

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We investigated the functional and selective activity of three phage-derived gold-binding peptides on the Escherichia coli (E. coli) bacterial cell surface display scaffold (eCPX) for the first time. Gold-binding peptides, p3-Au12 (LKAHLPPSRLPS), p8#9 (VSGSSPDS), and Midas-2 (TGTSVLIATPYV), were compared side-by-side through experiment and simulation. All exhibited strong binding to an evaporated gold film, with approximately a 4-log difference in binding between each peptide and the control sample. The increased affinity for gold was also confirmed by direct visualization of samples using Scanning Electron Microscopy (SEM). Peptide dynamics in solution were performed to analyze innate structure, and all three were found to have a high degree of flexibility. Preferential binding to gold over silicon for all three peptides was demonstrated, with up to four orders of magnitude selectivity exhibited by p3-Au12. The selectivity was also clearly evident through SEM analysis of the boundary between the gold film and silicon substrate. Functional activity of bound E. coli cells was further demonstrated by stimulating filamentation and all three peptides were characterized as prolific relative to control samples. This work shows great promise towards functional and active bacterial-hybrid gold surfaces and the potential to enable the next generation living material interfaces.

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Section: Surface Display Scaffoldsmentioning

confidence: 99%

Section: Surface Display Scaffoldsmentioning

confidence: 99%

Section: Gold-binding Peptidesmentioning

confidence: 99%

Section: Gold-binding Peptidesmentioning

confidence: 99%

Section: Surface Display Scaffoldsmentioning

confidence: 99%

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Functional and Selective Bacterial Interfaces Using Cross-Scaffold Gold Binding Peptides

Adams

Hurley

Jahnke

et al. 2015

JOM

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Discovery of Targeted Material Binding Microorganisms Using a Centrifugal Microfluidic Platform

Han

Sarkes

Jahnke

et al. 2021

Adv Materials Technologies

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Discovery of unique peptides that specifically bind to target materials of interest is commonly achieved through biopanning‐based screening of cell libraries having high diversity. However, conventional methods have limitations in the generation of controllable shear stress applied in order to effectively remove weak and unbound cells from a target material. Here, a centrifugal force‐based microfluidic biopanning platform is presented. Using this microfluidic platform, a wide range of shear stress conditions can be generated by simply adjusting the rotation speed of the platform, which provides a precisely controllable wash step. The enhanced circularly permuted outer membrane protein X (eCPX) 3.0 bacterial peptide display library (≈1011 number of cells) is screened, and many isolates that show strong affinity towards gold only, ITO only, or both are successfully obtained through a multiround iterative sorting process. Amino acid contents of the resulting isolates are analyzed to provide a better understanding of the distinctive attributes of these peptides and their specific material‐binding capabilities. This platform is simple and easy to use and can be readily applied to screen microbial libraries against virtually any material surface of interest, which can greatly accelerate the discovery of peptide‐driven biomaterials and the development of hybrid organic–inorganic materials.

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Peptide-driven assembly of Al/CuO energetic nanocomposite material

Song

Jin

Xian

et al. 2020

Chemical Engineering Journal

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Genetically Engineered Peptides for Inorganics: Study of an Unconstrained Bacterial Display Technology and Bulk Aluminum Alloy

Cited by 23 publications

References 45 publications

Functional and Selective Bacterial Interfaces Using Cross-Scaffold Gold Binding Peptides

Functional and Selective Bacterial Interfaces Using Cross-Scaffold Gold Binding Peptides

Discovery of Targeted Material Binding Microorganisms Using a Centrifugal Microfluidic Platform

Peptide-driven assembly of Al/CuO energetic nanocomposite material

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