Coding

Part:BBa_K3487002

Designed by: Jianhua Zhou   Group: iGEM20_SZPT-CHINA   (2020-10-09)
Revision as of 13:19, 18 October 2020 by LiuWanTing (Talk | contribs)

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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:
  • 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]

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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