Difference between revisions of "Part:BBa K3487002"
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<partinfo>BBa_K3487002 short</partinfo> | <partinfo>BBa_K3487002 short</partinfo> | ||
| + | ===Description=== | ||
North American frog isolated α helix cationic antimicrobial peptides a major role in the bacterial cell membrane, destruction of its integrity and produce perforation phenomenon, causing spillage of the contents extracellular cell death. We make use of its features to kill S. mutans in the mouth, to the effect of prevention and treatment. | North American frog isolated α helix cationic antimicrobial peptides a major role in the bacterial cell membrane, destruction of its integrity and produce perforation phenomenon, causing spillage of the contents extracellular cell death. We make use of its features to kill S. mutans in the mouth, to the effect of prevention and treatment. | ||
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| + | [[File:T--SZPT-CHINA--D4K.png|500px|thumb|center|We used D4K on Streptococcus mutans UA159 to test the antibacterial activity. Dilute the antimicrobial peptides to each experimental group. After culturing for 20 hours, scan the plate with a microplate reader at 490 nm. The MIC value of the antimicrobial peptide is determined to be calculated as the minimum mass concentration lower than 50% growth of the control well. Obtained 8μg/ml as the minimum inhibitory concentration of antimicrobial peptide against Streptococcus mutans. ]] | ||
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| + | ===Sequence and Features=== | ||
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| + | <partinfo>BBa_K3487002 SequenceAndFeatures</partinfo> | ||
| + | ===Reference=== | ||
| + | J. Michael Conlon, Agnes Sonnevend, Tibor Pál, et al. Efficacy of six frog skin-derived antimicrobial peptides against colistin-resistant strains of the Acinetobacter baumannii group. 2012, 39(4):317-320. | ||
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===Functional Parameters=== | ===Functional Parameters=== | ||
<partinfo>BBa_K3487002 parameters</partinfo> | <partinfo>BBa_K3487002 parameters</partinfo> | ||
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Latest revision as of 13:19, 18 October 2020
A bombesin
Description
North American frog isolated α helix cationic antimicrobial peptides a major role in the bacterial cell membrane, destruction of its integrity and produce perforation phenomenon, causing spillage of the contents extracellular cell death. We make use of its features to kill S. mutans in the mouth, to the effect of prevention and treatment.
We used D4K on Streptococcus mutans UA159 to test the antibacterial activity. Dilute the antimicrobial peptides to each experimental group. After culturing for 20 hours, scan the plate with a microplate reader at 490 nm. The MIC value of the antimicrobial peptide is determined to be calculated as the minimum mass concentration lower than 50% growth of the control well. Obtained 8μg/ml as the minimum inhibitory concentration of antimicrobial peptide against Streptococcus mutans.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Reference
J. Michael Conlon, Agnes Sonnevend, Tibor Pál, et al. Efficacy of six frog skin-derived antimicrobial peptides against colistin-resistant strains of the Acinetobacter baumannii group. 2012, 39(4):317-320.