Difference between revisions of "Team:WPI Worcester/Background"
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In terms of chemical structure, curcumin consists of a heptane backbone with phenyl groups at its terminal points. Moreover, two carbonyl groups, two methoxy groups, and two hydroxyl confer mild polarity to the molecule. The larger proportion of the aliphatic components make the substance mostly soluble in hydrophobic substances like oils and DMSO and amphyllic solvents like ethanol, and hardly soluble in water (“Curcumin”). Here is curcumin’s structure (“Curcumin”): | In terms of chemical structure, curcumin consists of a heptane backbone with phenyl groups at its terminal points. Moreover, two carbonyl groups, two methoxy groups, and two hydroxyl confer mild polarity to the molecule. The larger proportion of the aliphatic components make the substance mostly soluble in hydrophobic substances like oils and DMSO and amphyllic solvents like ethanol, and hardly soluble in water (“Curcumin”). Here is curcumin’s structure (“Curcumin”): | ||
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<figure> <p style="text-align:center"><img src="https://static.igem.org/mediawiki/2018/7/75/T--WPI_Worcester--Curcuminpoto.jpg" style="width: 300px;/> | <figure> <p style="text-align:center"><img src="https://static.igem.org/mediawiki/2018/7/75/T--WPI_Worcester--Curcuminpoto.jpg" style="width: 300px;/> | ||
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<figure> <p style="text-align:center"><img src="https://static.igem.org/mediawiki/2018/1/1f/T--WPI_Worcester--Curcuminplas.jpg" style="width: 300px;/> | <figure> <p style="text-align:center"><img src="https://static.igem.org/mediawiki/2018/1/1f/T--WPI_Worcester--Curcuminplas.jpg" style="width: 300px;/> | ||
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The second method, also by the Katsuyama group, is described in a later paper that serves as a refinement of the above procedure. The basis of the paper was to explore other CUS variants, with the CUS mentioned originating in rice (Katsuyama, 2009). To summarize, the paper outlines the discernment of two similar enzymes, diketide-CoA synthase (DCS) and curcumin synthase 1 (CURS1), both in the curcumina longa plant, that belong to an enzyme class labeled type III polyketide synthases (to which CUS is a member) (Katsuyama, 2009). The authors found that similar enzymes in the plant, CURS2 and CURS3, also produced curcumin in the plant’s roots (Katsuyama, 2009). To describe their methodology briefly, the authors used a pUC19 plasmid to subclone the cDNA genes for CURS2 and CURS3 with pET16b plasmid as the receiving vector for the translation of the genes with His tags for analysis with affinity chromatography using nickel ions (Katsuyama, 2009). The overall pathway is shown below in Fig 3, with DCS and CURS responsible for steps (3) and step (4), respectively: | The second method, also by the Katsuyama group, is described in a later paper that serves as a refinement of the above procedure. The basis of the paper was to explore other CUS variants, with the CUS mentioned originating in rice (Katsuyama, 2009). To summarize, the paper outlines the discernment of two similar enzymes, diketide-CoA synthase (DCS) and curcumin synthase 1 (CURS1), both in the curcumina longa plant, that belong to an enzyme class labeled type III polyketide synthases (to which CUS is a member) (Katsuyama, 2009). The authors found that similar enzymes in the plant, CURS2 and CURS3, also produced curcumin in the plant’s roots (Katsuyama, 2009). To describe their methodology briefly, the authors used a pUC19 plasmid to subclone the cDNA genes for CURS2 and CURS3 with pET16b plasmid as the receiving vector for the translation of the genes with His tags for analysis with affinity chromatography using nickel ions (Katsuyama, 2009). The overall pathway is shown below in Fig 3, with DCS and CURS responsible for steps (3) and step (4), respectively: | ||
Overall chemical reactions describing the second method are as follows: | Overall chemical reactions describing the second method are as follows: | ||
Revision as of 15:22, 15 October 2018
Background Information
Our biofilm experiments entailed the usage of different biologics, each possessing their own mechanism of production in vivo and chemistry. Here we summarize information from the scientific literature necessary for our experimental setups and provide a context in which our results may lie.
Curcumin
Antibiotic and Chemical Nature
Curcumin, the active ingredient of the spice turmeric, originates from the rhizome Curcuma longa. The compound possesses a yellow hue, and has been used in alternative medicine as an anti-inflammatory and antioxidant, and has recently been explored for potentially possessing an antibacterial ability (Tyagi, 2015). Curcumin apparently achieves its antibacterial nature from lysing the cell membranes of both Gram-positive and Gram-negative bacteria. Though the composition of bacterial types differ, this compound perforates bacterial membranes to allow the contents of each cell type to eject into the extracellular space, thereby killing the cells in the process. Specifically, by virtue of possessing an amphipathic chemistry, curcumin can selectively insert into lipid bilayers and disrupt the native structure (Tyagi, 2015). As biofilms develop through quorum sensing mechanisms (the communication pathways between bacteria that selectively activates gene transcription via signaling molecules), the breakdown of cellular membranes does away the entryways of such molecules (Solano,2014). Therefore, if bacteria survive initial membrane perforation, they lose the ability to accurately secrete and absorb signaling molecules to further biofilm growth (“What is QS?”). In terms of chemical structure, curcumin consists of a heptane backbone with phenyl groups at its terminal points. Moreover, two carbonyl groups, two methoxy groups, and two hydroxyl confer mild polarity to the molecule. The larger proportion of the aliphatic components make the substance mostly soluble in hydrophobic substances like oils and DMSO and amphyllic solvents like ethanol, and hardly soluble in water (“Curcumin”). Here is curcumin’s structure (“Curcumin”):
