@article {3044,
	title = {Microbial nanowires with genetically modified peptide ligands to sustainably fabricate electronic sensing devices.},
	journal = {Biosens Bioelectron},
	volume = {226},
	year = {2023},
	month = {2023 Apr 15},
	pages = {115147},
	abstract = {<p>Nanowires have substantial potential as the sensor component in electronic sensing devices. However, surface functionalization of traditional nanowire and nanotube materials with short peptides that increase sensor selectivity and sensitivity requires complex chemistries with toxic reagents. In contrast, microorganisms can assemble pilin monomers into protein nanowires with intrinsic conductivity from renewable feedstocks, yielding an electronic material that is robust and stable in applications, but also biodegradable. Here we report that the sensitivity and selectivity of protein nanowire-based sensors can be modified with a simple plug and play genetic approach in which a short peptide sequence, designed to bind the analyte of interest, is incorporated into the pilin protein that is microbially assembled into nanowires. We employed a scalable Escherichia coli chassis to fabricate protein nanowires that displayed either a peptide previously demonstrated to effectively bind ammonia, or a peptide known to bind acetic acid. Sensors comprised of thin films of the nanowires amended with the ammonia-specific peptide had a ca. 100-fold greater response to ammonia than sensors made with unmodified protein nanowires. Protein nanowires with the peptide that binds acetic acid yielded a 4-fold higher response than nanowires without the peptide. The protein nanowire-based sensors had greater responses than previously reported sensors fabricated with other nanomaterials. The results demonstrate that protein nanowires with enhanced sensor response for analytes of interest can be fabricated with a flexible genetic strategy that sustainably eliminates the energy, environmental, and health concerns associated with other common nanomaterials.</p>},
	keywords = {Acetic Acid, Ammonia, Biosensing Techniques, Electronics, Fimbriae Proteins, Ligands, Nanowires, Peptides},
	issn = {1873-4235},
	doi = {10.1016/j.bios.2023.115147},
	author = {Lekbach, Yassir and Ueki, Toshiyuki and Liu, Xiaomeng and Woodard, Trevor and Yao, Jun and Lovley, Derek R}
}
@article {690,
	title = {Direct recognition of the mycobacterial glycolipid, trehalose dimycolate, by C-type lectin Mincle.},
	journal = {J Exp Med},
	volume = {206},
	year = {2009},
	month = {2009 Dec 21},
	pages = {2879-88},
	abstract = {Tuberculosis remains a fatal disease caused by Mycobacterium tuberculosis, which contains various unique components that affect the host immune system. Trehalose-6,6{\textquoteright}-dimycolate (TDM; also called cord factor) is a mycobacterial cell wall glycolipid that is the most studied immunostimulatory component of M. tuberculosis. Despite five decades of research on TDM, its host receptor has not been clearly identified. Here, we demonstrate that macrophage inducible C-type lectin (Mincle) is an essential receptor for TDM. Heat-killed mycobacteria activated Mincle-expressing cells, but the activity was lost upon delipidation of the bacteria; analysis of the lipid extracts identified TDM as a Mincle ligand. TDM activated macrophages to produce inflammatory cytokines and nitric oxide, which are completely suppressed in Mincle-deficient macrophages. In vivo TDM administration induced a robust elevation of inflammatory cytokines in sera and characteristic lung inflammation, such as granuloma formation. However, no TDM-induced lung granuloma was formed in Mincle-deficient mice. Whole mycobacteria were able to activate macrophages even in MyD88-deficient background, but the activation was significantly diminished in Mincle/MyD88 double-deficient macrophages. These results demonstrate that Mincle is an essential receptor for the mycobacterial glycolipid, TDM.},
	keywords = {Animals, Cord Factors, Granuloma, Lectins, C-Type, Ligands, Lung Diseases, Macrophage Activation, Membrane Proteins, Mice, Mice, Inbred C57BL, Myeloid Differentiation Factor 88, Receptors, IgG},
	issn = {1540-9538},
	doi = {10.1084/jem.20091750},
	author = {Ishikawa, Eri and Ishikawa, Tetsuaki and Morita, Yasu S and Toyonaga, Kenji and Yamada, Hisakata and Takeuchi, Osamu and Kinoshita, Taroh and Akira, Shizuo and Yoshikai, Yasunobu and Yamasaki, Sho}
}
@article {643,
	title = {Stimulated anoxic biodegradation of aromatic hydrocarbons using Fe(III) ligands.},
	journal = {Nature},
	volume = {370},
	year = {1994},
	month = {1994 Jul 14},
	pages = {128-31},
	abstract = {Contamination of ground waters with water-soluble aromatic hydrocarbons, common components of petroleum pollution, often produces anoxic conditions under which microbial degradation of the aromatics is slow. Oxygen is often added to contaminated ground water to stimulate biodegradation, but this can be technically difficult and expensive. Insoluble Fe(III) oxides, which are generally abundant in shallow aquifers, are alternative potential oxidants, but are difficult for microorganisms to access. Here we report that adding organic ligands that bind to Fe(III) dramatically increases its bioavailability, and that in the presence of these ligands, rates of degradation of aromatic hydrocarbons in anoxic aquifer sediments are comparable to those in oxic sediments. We find that even benzene, which is notoriously refractory in the absence of oxygen, can be rapidly degraded. Our results suggest that increasing the bioavailability of Fe(III) by adding suitable ligands provides a potential alternative to oxygen addition for the bioremediation of petroleum-contaminated aquifers.},
	keywords = {Benzene, Biodegradation, Environmental, Ferric Compounds, Hydrocarbons, Ligands, Methane, Nitrilotriacetic Acid, Oxidation-Reduction, Toluene, Water Pollutants, Chemical},
	issn = {0028-0836},
	doi = {10.1038/370128a0},
	author = {Lovley, D R and Woodward, J C and Chapelle, F H}
}
@article {1726,
	title = {Studies of oxygen binding energy to hemoglobin molecule.},
	journal = {Biochem Biophys Res Commun},
	volume = {66},
	year = {1975},
	month = {1975 Oct 27},
	pages = {1424-31},
	keywords = {Binding Sites, Cobalt, Hemoglobins, Humans, Hydrogen-Ion Concentration, Iron, Ligands, Mathematics, Oxygen, Oxyhemoglobins, Protein Binding, Spectrum Analysis},
	issn = {0006-291X},
	author = {Chow, Y W and Pietranico, R and Mukerji, A}
}
