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Article ; Online: Building a biofoundry.

Holowko, Maciej B / Frow, Emma K / Reid, Janet C / Rourke, Michelle / Vickers, Claudia E

Synthetic biology (Oxford, England)

2020 Volume 6, Issue 1, Page(s) ysaa026

Abstract: A biofoundry provides automation and analytics infrastructure to support the engineering of biological systems. It allows scientists to perform synthetic biology and aligned experimentation on a high-throughput scale, massively increasing the solution ... ...

Abstract	A biofoundry provides automation and analytics infrastructure to support the engineering of biological systems. It allows scientists to perform synthetic biology and aligned experimentation on a high-throughput scale, massively increasing the solution space that can be examined for any given problem or question. However, establishing a biofoundry is a challenging undertaking, with numerous technical and operational considerations that must be addressed. Using collated learnings, here we outline several considerations that should be addressed prior to and during establishment. These include drivers for establishment, institutional models, funding and revenue models, personnel, hardware and software, data management, interoperability, client engagement and biosecurity issues. The high cost of establishment and operation means that developing a long-term business model for biofoundry sustainability in the context of funding frameworks, actual and potential client base, and costing structure is critical. Moreover, since biofoundries are leading a conceptual shift in experimental design for bioengineering, sustained outreach and engagement with the research community are needed to grow the client base. Recognition of the significant, long-term financial investment required and an understanding of the complexities of operationalization is critical for a sustainable biofoundry venture. To ensure state-of-the-art technology is integrated into planning, extensive engagement with existing facilities and community groups, such as the Global Biofoundries Alliance, is recommended.
Language	English
Publishing date	2020-12-16
Publishing country	England
Document type	Journal Article ; Review
ISSN	2397-7000
ISSN (online)	2397-7000
DOI	10.1093/synbio/ysaa026
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Article ; Online: Evidence that cell surface localization of serine protease activity facilitates cleavage of the protease activated receptor CDCP1.

He, Yaowu / Reid, Janet C / He, Hui / Harrington, Brittney S / Finlayson, Brittney / Khan, Tashbib / Hooper, John D

Biological chemistry

2018 Volume 399, Issue 9, Page(s) 1091–1097

Abstract: The cellular receptor CUB domain containing protein 1 (CDCP1) is commonly elevated and functionally important in a range of cancers. CDCP1 is cleaved by serine proteases at adjacent sites, arginine 368 (R368) and lysine 369 (K369), which induces cell ... ...

Abstract	The cellular receptor CUB domain containing protein 1 (CDCP1) is commonly elevated and functionally important in a range of cancers. CDCP1 is cleaved by serine proteases at adjacent sites, arginine 368 (R368) and lysine 369 (K369), which induces cell migration in vitro and metastasis in vivo. We demonstrate that membrane localization of serine protease activity increases efficacy of cleavage of CDCP1, and that both secreted and membrane anchored serine proteases can have distinct preferences for cleaving at CDCP1-R368 and CDCP1-K369. Approaches that disrupt membrane localization of CDCP1 cleaving serine proteases may interfere with the cancer promoting effects of CDCP1 proteolysis.
MeSH term(s)	Antigens, CD/metabolism ; Cell Adhesion Molecules/metabolism ; Cell Line, Tumor ; Cell Membrane/enzymology ; Cell Movement ; Humans ; Kidney Neoplasms/metabolism ; Kidney Neoplasms/pathology ; Neoplasm Proteins/metabolism ; Proteolysis ; Receptors, Proteinase-Activated/metabolism ; Serine Proteases/metabolism
Chemical Substances	Antigens, CD ; CDCP1 protein, human ; Cell Adhesion Molecules ; Neoplasm Proteins ; Receptors, Proteinase-Activated ; Serine Proteases (EC 3.4.-)
Language	English
Publishing date	2018-02-15
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1334659-3
ISSN	1437-4315 ; 1431-6730 ; 1432-0355
ISSN (online)	1437-4315
ISSN	1431-6730 ; 1432-0355
DOI	10.1515/hsz-2017-0308
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Article ; Online: Antitubercular and Antiparasitic 2-Nitroimidazopyrazinones with Improved Potency and Solubility.

Ang, Chee Wei / Tan, Lendl / Sykes, Melissa L / AbuGharbiyeh, Neda / Debnath, Anjan / Reid, Janet C / West, Nicholas P / Avery, Vicky M / Cooper, Matthew A / Blaskovich, Mark A T

Journal of medicinal chemistry

2020 Volume 63, Issue 24, Page(s) 15726–15751

Abstract: Following the approval of delamanid and pretomanid as new drugs to treat drug-resistant tuberculosis, there is now a renewed interest in bicyclic nitroimidazole scaffolds as a source of therapeutics against infectious diseases. We recently described a ... ...

Abstract	Following the approval of delamanid and pretomanid as new drugs to treat drug-resistant tuberculosis, there is now a renewed interest in bicyclic nitroimidazole scaffolds as a source of therapeutics against infectious diseases. We recently described a nitroimidazopyrazinone bicyclic subclass with promising antitubercular and antiparasitic activity, prompting additional efforts to generate analogs with improved solubility and enhanced potency. The key pendant aryl substituent was modified by (i) introducing polar functionality to the methylene linker, (ii) replacing the terminal phenyl group with less lipophilic heterocycles, or (iii) generating extended biaryl side chains. Improved antitubercular and antitrypanosomal activity was observed with the biaryl side chains, with most analogs achieved 2- to 175-fold higher activity than the monoaryl parent compounds, with encouraging improvements in solubility when pyridyl groups were incorporated. This study has contributed to understanding the existing structure-activity relationship (SAR) of the nitroimidazopyrazinone scaffold against a panel of disease-causing organisms to support future lead optimization.
MeSH term(s)	Animals ; Antiprotozoal Agents/chemistry ; Antiprotozoal Agents/pharmacology ; Antitubercular Agents/chemistry ; Antitubercular Agents/metabolism ; Antitubercular Agents/pharmacology ; Blood Proteins/chemistry ; Blood Proteins/metabolism ; Cell Survival/drug effects ; Drug Design ; Half-Life ; Humans ; Mice ; Microbial Sensitivity Tests ; Microsomes/metabolism ; Mycobacterium/drug effects ; Nitroimidazoles/chemistry ; Protein Binding ; Pyrazines/chemistry ; Pyrazines/metabolism ; Pyrazines/pharmacology ; Solubility ; Structure-Activity Relationship ; Trypanosoma brucei brucei/drug effects
Chemical Substances	Antiprotozoal Agents ; Antitubercular Agents ; Blood Proteins ; Nitroimidazoles ; Pyrazines
Language	English
Publishing date	2020-11-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	218133-2
ISSN	1520-4804 ; 0022-2623
ISSN (online)	1520-4804
ISSN	0022-2623
DOI	10.1021/acs.jmedchem.0c01372
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Article ; Online: Synthesis of deuterium-labelled analogues of NLRP3 inflammasome inhibitor MCC950.

Salla, Manohar / Butler, Mark S / Massey, Nicholas L / Reid, Janet C / Cooper, Matthew A / Robertson, Avril A B

Bioorganic & medicinal chemistry letters

2017 Volume 28, Issue 4, Page(s) 793–795

Abstract: This study describes the syntheses of di, tetra and hexa deuterated analogues of the NOD-like receptor pyrin domain-containing protein 3 (NLRP3) inflammasome inhibitor MCC950. In di and tetra deuterated analogues, deuteriums were incorporated into the 1, ... ...

Abstract	This study describes the syntheses of di, tetra and hexa deuterated analogues of the NOD-like receptor pyrin domain-containing protein 3 (NLRP3) inflammasome inhibitor MCC950. In di and tetra deuterated analogues, deuteriums were incorporated into the 1,2,3,5,6,7-hexahydro-s-indacene moiety, whereas in the hexa deuterated MCC950 deuteriums were incorporated into the 2-(furan-3-yl)propan-2-ol moiety. The di deuterated MCC950 analogue was synthesised from 4-amino-3,5,6,7-tetrahydro-s-indacen-1(2H)-one 5. Tetra deuterated analogues were synthesised in 10 chemical steps starting with 5-bromo-2,3-dihydro-1H-inden-1-one 9, whereas the hexa deuterated analogue was synthesised in four chemical steps starting with ethyl-3-furoate 24. All of the compounds exhibited similar activity to MCC950 (IC
MeSH term(s)	Chromatography, Liquid/methods ; Deuterium ; Furans ; Heterocyclic Compounds, 4 or More Rings/chemical synthesis ; Heterocyclic Compounds, 4 or More Rings/chemistry ; Heterocyclic Compounds, 4 or More Rings/pharmacokinetics ; Humans ; Indenes ; Inflammasomes/antagonists & inhibitors ; Interleukin-1beta/metabolism ; Macrophages/metabolism ; Mass Spectrometry/methods ; NLR Family, Pyrin Domain-Containing 3 Protein/antagonists & inhibitors ; Reference Standards ; Sulfonamides ; Sulfones/chemical synthesis ; Sulfones/chemistry ; Sulfones/pharmacokinetics
Chemical Substances	Furans ; Heterocyclic Compounds, 4 or More Rings ; Indenes ; Inflammasomes ; Interleukin-1beta ; NLR Family, Pyrin Domain-Containing 3 Protein ; Sulfonamides ; Sulfones ; N-(1,2,3,5,6,7-hexahydro-S-indacen-4-ylcarbamoyl)-4-(2-hydroxy-2-propanyl)-2-furansulfonamide (6RS86E2BWQ) ; Deuterium (AR09D82C7G)
Language	English
Publishing date	2017-12-26
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1063195-1
ISSN	1464-3405 ; 0960-894X
ISSN (online)	1464-3405
ISSN	0960-894X
DOI	10.1016/j.bmcl.2017.12.054
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Article ; Online: In vitro evidence that KLK14 regulates the components of the HGF/Met axis, pro-HGF and HGF-activator inhibitor 1A and 1B.

Reid, Janet C / Bennett, Nigel C / Stephens, Carson R / Carroll, Melanie L / Magdolen, Viktor / Clements, Judith A / Hooper, John D

Biological chemistry

2016 Volume 397, Issue 12, Page(s) 1299–1305

Abstract: Kallikrein-related peptidase (KLK) 14 is a serine protease linked to several pathologies including prostate cancer. We show that KLK14 has biphasic effects in vitro on activating and inhibiting components of the prostate cancer associated hepatocyte ... ...

Abstract	Kallikrein-related peptidase (KLK) 14 is a serine protease linked to several pathologies including prostate cancer. We show that KLK14 has biphasic effects in vitro on activating and inhibiting components of the prostate cancer associated hepatocyte growth factor (HGF)/Met system. At 5-10 nm, KLK14 converts pro-HGF to the two-chain heterodimer required for Met activation, while higher concentrations degrade the HGF α-chain. HGF activator-inhibitor (HAI)-1A and HAI-1B, which inhibit pro-HGF activators, are degraded by KLK14 when protease:inhibitor stoichiometry is 1:1 or the protease is in excess. When inhibitors are in excess, KLK14 generates HAI-1A and HAI-1B fragments known to inhibit pro-HGF activating serine proteases. These in vitro data suggest that increased KLK14 activity could contribute at multiple levels to HGF/Met-mediated processes in prostate and other cancers.
MeSH term(s)	Animals ; Hepatocyte Growth Factor/metabolism ; Humans ; Male ; Prostatic Neoplasms/metabolism ; Protein Precursors/metabolism ; Proteinase Inhibitory Proteins, Secretory/metabolism ; Proto-Oncogene Proteins c-met/metabolism ; Sf9 Cells ; Spodoptera
Chemical Substances	Protein Precursors ; Proteinase Inhibitory Proteins, Secretory ; pro-hepatocyte growth factor ; Hepatocyte Growth Factor (67256-21-7) ; Proto-Oncogene Proteins c-met (EC 2.7.10.1)
Language	English
Publishing date	2016-12-01
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1334659-3
ISSN	1437-4315 ; 1431-6730 ; 1432-0355
ISSN (online)	1437-4315
ISSN	1431-6730 ; 1432-0355
DOI	10.1515/hsz-2016-0163
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Article ; Online: An optimised Cu(0)-RDRP approach for the synthesis of lipidated oligomeric vinyl azlactone: toward a versatile antimicrobial materials screening platform.

Grace, James L / Amado, Maite / Reid, Janet C / Elliott, Alysha G / Landersdorfer, Cornelia B / Truong, Nghia P / Kempe, Kristian / Cooper, Matthew A / Davis, Thomas P / Montembault, Véronique / Pascual, Sagrario / Fontaine, Laurent / Velkov, Tony / Quinn, John F / Whittaker, Michael R

Journal of materials chemistry. B

2019 Volume 7, Issue 43, Page(s) 6796–6809

Abstract: This report details the synthesis of lipidated 2-vinyl-4,4-dimethyl-5-oxazolone (VDM) oligomers via an optimised Cu(0)-mediated reversible-deactivation radical polymerisation approach, and the use of these oligomers as a versatile functional platform for ...

Abstract	This report details the synthesis of lipidated 2-vinyl-4,4-dimethyl-5-oxazolone (VDM) oligomers via an optimised Cu(0)-mediated reversible-deactivation radical polymerisation approach, and the use of these oligomers as a versatile functional platform for the rapid generation of antimicrobial materials. The relative amounts of CuBr
MeSH term(s)	Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/therapeutic use ; Molecular Structure ; Polyvinyl Chloride/chemistry ; Structure-Activity Relationship
Chemical Substances	Anti-Bacterial Agents ; Polyvinyl Chloride (9002-86-2)
Language	English
Publishing date	2019-10-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2702241-9
ISSN	2050-7518 ; 2050-750X
ISSN (online)	2050-7518
ISSN	2050-750X
DOI	10.1039/c9tb01624d
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Article: Pericellular regulation of prostate cancer expressed kallikrein-related peptidases and matrix metalloproteinases by cell surface serine proteases.

Reid, Janet C / Matsika, Admire / Davies, Claire M / He, Yaowu / Broomfield, Amy / Bennett, Nigel C / Magdolen, Viktor / Srinivasan, Bhuvana / Clements, Judith A / Hooper, John D

American journal of cancer research

2017 Volume 7, Issue 11, Page(s) 2257–2274

Abstract: We provide evidence of a pericellular network of proteases that are elevated and co-expressed in prostate cancer. The network involves the membrane bound serine proteases hepsin and TMPRSS2, the secreted kallikrein-related peptidases KLK4 and KLK14, and ... ...

Abstract	We provide evidence of a pericellular network of proteases that are elevated and co-expressed in prostate cancer. The network involves the membrane bound serine proteases hepsin and TMPRSS2, the secreted kallikrein-related peptidases KLK4 and KLK14, and the secreted matrix metalloproteinases MMP-3 and MMP-9. Western blot analysis of cell lysates, conditioned cell culture media, immunoprecipitates and cell surface proteins, demonstrates a network of interactions centred largely at the plasma membrane, with the Arg/Lys specific proteases hepsin and TMPRSS2 key regulators of the network. Our data demonstrate that like TMPRSS2, hepsin is able to autoactivate. Active hepsin degrades KLK4, generating a cell associated degradation product with corresponding reduction in levels of cell-free KLK4. In contrast hepsin activates KLK14. TMPRSS2 appears to cleave amino terminal to the KLK4 activation site such that it is available for further processing to generate the active KLK4 protease. In contrast with hepsin, TMPRSS2 degrades KLK14. In addition to these direct mechanisms of regulation, hepsin and TMPRSS2 indirectly modulate KLK4 activity by cleaving the KLK4-activating protease MMP-3. Hepsin and TMPRSS2 also activate MMP-9, which similar to MMP-3, associates with the cell surface. Interestingly our data also show that proteolysis occurs between the membrane spanning and catalytic domains of hepsin and TMPRSS2. Hepsin cleavage occurs via an autoproteolytic mechanism, whereas TMPRSS2 cleavage is mediated by KLK14. Hepsin and TMPRSS2 are not shed from the cell surface but proteolysis likely disrupts domains that regulate the proteolytic activity of these proteases. Immunocytochemical analyses demonstrate that hepsin and TMPRSS2 colocalize on the cell surface with the secreted serine proteases KLK4 and KLK14, only in membrane protrusions, suggesting that reciprocal proteolytic interactions occur in defined cellular structures that are important during cancer dissemination for cell migration, invasion and survival. Also of note, immunohistochemical analysis of serial sections of prostate tumor demonstrated significant overlapping expression of the six proteases
Language	English
Publishing date	2017-11-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	2589522-9
ISSN	2156-6976
ISSN	2156-6976
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Article ; Online: Sulfonylureas as Concomitant Insulin Secretagogues and NLRP3 Inflammasome Inhibitors.

Hill, James R / Coll, Rebecca C / Sue, Nancy / Reid, Janet C / Dou, Jennifer / Holley, Caroline L / Pelingon, Ruby / Dickinson, Joshua B / Biden, Trevor J / Schroder, Kate / Cooper, Matthew A / Robertson, Avril A B

ChemMedChem

2017 Volume 12, Issue 17, Page(s) 1449–1457

Abstract: Insulin-secretory sulfonylureas are widely used, cost-effective treatments for type 2 diabetes (T2D). However, pancreatic β-cells are continually depleted as T2D progresses, thereby rendering the sulfonylurea drug class ineffective in controlling ... ...

Abstract	Insulin-secretory sulfonylureas are widely used, cost-effective treatments for type 2 diabetes (T2D). However, pancreatic β-cells are continually depleted as T2D progresses, thereby rendering the sulfonylurea drug class ineffective in controlling glycaemia. Dysregulation of the innate immune system via activation of the NLRP3 inflammasome, and the consequent production of interleukin-1β, has been linked to pancreatic β-cell death and multiple inflammatory complications of T2D disease. One proposed strategy for treating T2D is the use of sulfonylurea insulin secretagogues that are also NLRP3 inhibitors. We report the synthesis and biological evaluation of nine sulfonylureas that inhibit NLRP3 activation in murine bone-marrow- derived macrophages in a potent, dose-dependent manner. Six of these compounds inhibited NLRP3 at nanomolar concentrations and can also stimulate insulin secretion from a murine pancreatic cell line (MIN6). These novel compounds possess unprecedented dual modes of action, paving the way for a new generation of sulfonylureas that may be useful as therapeutic candidates and/or tool compounds in T2D and its associated inflammatory complications.
MeSH term(s)	Animals ; Cell Line ; Cells, Cultured ; Diabetes Mellitus, Type 2/drug therapy ; Diabetes Mellitus, Type 2/immunology ; HEK293 Cells ; Humans ; Hypoglycemic Agents/chemistry ; Hypoglycemic Agents/pharmacology ; Inflammasomes/antagonists & inhibitors ; Inflammasomes/immunology ; Insulin/immunology ; Mice, Inbred C57BL ; NLR Family, Pyrin Domain-Containing 3 Protein/antagonists & inhibitors ; NLR Family, Pyrin Domain-Containing 3 Protein/immunology ; Pancreas/cytology ; Pancreas/drug effects ; Pancreas/immunology ; Sulfonylurea Compounds/chemistry ; Sulfonylurea Compounds/pharmacology
Chemical Substances	Hypoglycemic Agents ; Inflammasomes ; Insulin ; NLR Family, Pyrin Domain-Containing 3 Protein ; Sulfonylurea Compounds
Language	English
Publishing date	2017-09-07
Publishing country	Germany
Document type	Journal Article
ZDB-ID	2218496-X
ISSN	1860-7187 ; 1860-7179
ISSN (online)	1860-7187
ISSN	1860-7179
DOI	10.1002/cmdc.201700270
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Article: An optimised Cu(0)-RDRP approach for the synthesis of lipidated oligomeric vinyl azlactone: toward a versatile antimicrobial materials screening platform

Grace, James L / Amado, Maite / Cooper, Matthew A / Davis, Thomas P / Elliott, Alysha G / Fontaine, Laurent / Kempe, Kristian / Landersdorfer, Cornelia B / Montembault, Véronique / Pascual, Sagrario / Quinn, John F / Reid, Janet C / Truong, Nghia P / Velkov, Tony / Whittaker, Michael R

Journal of materials chemistry B. 2019 Nov. 6, v. 7, no. 43

2019

Abstract	This report details the synthesis of lipidated 2-vinyl-4,4-dimethyl-5-oxazolone (VDM) oligomers via an optimised Cu(0)-mediated reversible-deactivation radical polymerisation approach, and the use of these oligomers as a versatile functional platform for the rapid generation of antimicrobial materials. The relative amounts of CuBr2 and Me6TREN were optimised to allow the fast and controlled polymerisation of VDM. These conditions were then used with the initiators ethyl 2-bromoisobutyrate, dodecyl 2-bromoisobutyrate, and (R)-3-((2-bromo-2-methylpropanoyl)oxy)propane-1,2-diyl didodecanoate to synthesise a library of oligo(VDM) (degree of polymerisation = 10) with ethyl, dodecyl or diglyceride end-groups. Subsequently, ring-opening of the pendant oxazolone group with various amines (i.e., 2-(2-aminoethyl)-1,3-di-Boc-guanidine, 1-(3-aminopropyl)imidazole, N-Boc-ethylenediamine, or N,N-dimethylethylenediamine) expanded the library to give 12 functional oligomers incorporating different cationic and lipid elements. The antimicrobial activities of these oligomers were assessed against a palette of bacteria and fungi: i.e. Staphylococcus aureus, Escherichia coli, Candida albicans, and Cryptococcus neoformans. The oligomers generally exhibited the greatest activity against the fungus, C. neoformans, with a minimum inhibitory concentration of 1 μg mL−1 (comparable to the clinically approved antifungal fluconazole). To assess haemocompatibility, the oligomers were assayed against erythrocytes, with the primary amine or guanidine containing C12 and 2C12 oligomers exhibiting greater lysis against the red blood cells (HC10 values between 7.1 and 43 μg mL−1) than their imidazole and tertiary amine counterparts (HC10 of >217 μg mL−1). Oligomers showed the greatest selectivity for C. neoformans, with the C12- and 2C12-tertiary amine and C12-imidazole oligomers possessing the greatest selectivity of >54–109. These results demonstrate the utility of reactive oligomers for rapidly assessing structure–property relationships for antibacterial and antifungal materials.
Keywords	amines ; antimicrobial properties ; Candida albicans ; copper ; Cryptococcus neoformans ; diacylglycerols ; erythrocytes ; Escherichia coli ; fluconazole ; fungi ; guanidines ; imidazole ; lactones ; minimum inhibitory concentration ; polymerization ; screening ; Staphylococcus aureus
Language	English
Dates of publication	2019-1106
Size	p. 6796-6809.
Publishing place	The Royal Society of Chemistry
Document type	Article
ZDB-ID	2702241-9
ISSN	2050-7518 ; 2050-750X
ISSN (online)	2050-7518
ISSN	2050-750X
DOI	10.1039/c9tb01624d
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Article: Identification, Synthesis, and Biological Evaluation of the Major Human Metabolite of NLRP3 Inflammasome Inhibitor MCC950.

Salla, Manohar / Butler, Mark S / Pelingon, Ruby / Kaeslin, Geraldine / Croker, Daniel E / Reid, Janet C / Baek, Jong Min / Bernhardt, Paul V / Gillam, Elizabeth M J / Cooper, Matthew A / Robertson, Avril A B

ACS medicinal chemistry letters

2016 Volume 7, Issue 12, Page(s) 1034–1038

Abstract: MCC950 is an orally bioavailable small molecule inhibitor of the NOD-like receptor pyrin domain-containing protein 3 (NLRP3) inflammasome that exhibits remarkable activity in multiple models of inflammatory disease. Incubation of MCC950 with human liver ... ...

Abstract	MCC950 is an orally bioavailable small molecule inhibitor of the NOD-like receptor pyrin domain-containing protein 3 (NLRP3) inflammasome that exhibits remarkable activity in multiple models of inflammatory disease. Incubation of MCC950 with human liver microsomes, and subsequent analysis by HPLC-MS/MS, revealed a major metabolite, where hydroxylation of MCC950 had occurred on the 1,2,3,5,6,7-hexahydro-
Language	English
Publishing date	2016-09-27
Publishing country	United States
Document type	Journal Article
ISSN	1948-5875
ISSN	1948-5875
DOI	10.1021/acsmedchemlett.6b00198
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