Difference between revisions of "Part:BBa K3182010"

Latest revision as of 17:19, 21 October 2019

Parseq-β

Parseq Beta is a de novo antimicrobial peptide. It was generated by the Parseq model and the antimicrobial activity was predicted by the Parseq model. This part was first ordered chemically synthesized by Caslo to investigate its antimicrobial activity on its own. The peptides were dissolved in 6 M Urea due to their hydrophobic nature. The activity was tested on E.coli and B.Subtilis. The antimicrobial activity assay was carried out in a 96 well plate. Bacteria were combined with the antimicrobial peptides in different concentrations. They were then incubated at 37°C, with shaking, every 15 minutes. The plate was incubated for 16 hours and OD₆₀₀ was measured. The results can be seen in Figure 1. Parseq Beta showed an inhibiting effect on the growth of E.coli. A concentration of 100 µg/mL completely inhibited the growth of E.coli. B.subtilis could not be inhibited completely by Parseq Beta. However, high concentrations of the peptide showed partial inhibition of the growth of B.subtilis.

Figure 1. Shows the antimicrobial activity of Parseq Beta on A) E.Coli. and B) B.subtilis. The samples were cultured in 200 µL low salt LB, in a 96 well plate and incubated at 37°C. Shaking was conducted for 1 minute every 15 minutes and the OD₆₀₀ was measured every hour for 16 hours. The negative control represents the bacterial growth with no antimicrobial peptides present. All measurements are done in 6 replicates (except for BSA for B.subtilis which had 5 replicates) and error bars represent SD. The graphs were created in Graphpad

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

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 <partinfo>BBa_K3182010 short</partinfo>
-This part is a de novo antimicrobial peptide. The antimicrobial peptide was generated by the Parseq model and the antimicrobial activity was predicted by the Parseq model. This part was designed to be assembled with BBa_K3182010.
+Parseq Beta is a de novo antimicrobial peptide. It was generated by the Parseq model and the antimicrobial activity was predicted by the Parseq model. This part was first ordered chemically synthesized by Caslo to investigate its antimicrobial activity on its own. The peptides were dissolved in 6 M Urea due to their hydrophobic nature. The activity was tested on <i>E.coli</i> and <i>B.Subtilis</i>. The antimicrobial activity assay was carried out in a 96 well plate. Bacteria were combined with the antimicrobial peptides in different concentrations. They were then incubated at 37°C, with shaking, every 15 minutes. The plate was incubated for 16 hours and OD<sub>600</sub> was measured. The results can be seen in <b>Figure 1.</b> Parseq Beta showed an inhibiting effect on the growth of <i>E.coli</i>. A concentration of 100 µg/mL completely inhibited the growth of <i>E.coli</i>. <i>B.subtilis</i> could not be inhibited completely by Parseq Beta. However, high concentrations of the peptide showed partial inhibition of the growth of <i>B.subtilis</i>.
+[[File:T--Linkoping_Sweden--BETAAA.png|650px|thumb|center| <b>Figure 1.</b> Shows the antimicrobial activity of Parseq Beta on A) <i>E.Coli.</i> and B) <i>B.subtilis</i>. The samples were cultured in 200 µL low salt LB, in a 96 well plate and incubated at 37°C. Shaking was conducted for 1 minute every 15 minutes and the OD<sub>600</sub> was measured every hour for 16 hours. The negative control represents the bacterial growth with no antimicrobial peptides present. All measurements are done in 6 replicates (except for BSA for <i>B.subtilis</i> which had 5 replicates) and error bars represent SD. The graphs were created in Graphpad]]
-[[File:T--Linkoping_Sweden--MechofAction.png|650px|thumb|center|<b>Figure 1.</b> General mechanism of action when the antimicrobial agent is fused to BBa_K3182010 which contains the linker, thrombin site and cellulose binding domain. The cellulose binding domain enables the attachment of antimicrobial agents (such as antimicrobial peptide or enzyme) to the cellulose. This also inactivates the agents when they are expressed in its bacterial host. Later, when the bandage comes in contact with thrombin in the blood, the antimicrobial agents will be activated upon cleavage of its thrombin site.]]
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