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Meeting Abstracts. Recent Developments in 1,3-beta-Glucan Biology: Proceedings of the 5th Glucan Symposium Tokyo, December 8, 2006.

- Mediators Inflamm. (2007)

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Hydrophilicity/hydrophobicity plots of LL-37 and its 18-mer peptide derivatives.
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Related In: Results  -  Collection


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fig8-5: Hydrophilicity/hydrophobicity plots of LL-37 and its 18-mer peptide derivatives.

Mentions: Antibacterial activities of the peptides were assessed by alamarBlue assay using Staphylococcus aureus (MSSA, meth- icillin-sensitive Staphylococcus aureus; MRSA methicillin-resistant Staphylococcus aureus), Escherichia coli, Streptococcus pneumoniae, Streptococcus pyogenes, and Pseudomonas aeruginosa as target organisms [1]. The 18-mer peptides as well as LL-37 inhibited the growth of these bacteria, and 18-mer LLKKK was the most potent among the peptide derivatives (Figure 5).


Meeting Abstracts. Recent Developments in 1,3-beta-Glucan Biology: Proceedings of the 5th Glucan Symposium Tokyo, December 8, 2006.

- Mediators Inflamm. (2007)

Hydrophilicity/hydrophobicity plots of LL-37 and its 18-mer peptide derivatives.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2327214&req=5

fig8-5: Hydrophilicity/hydrophobicity plots of LL-37 and its 18-mer peptide derivatives.
Mentions: Antibacterial activities of the peptides were assessed by alamarBlue assay using Staphylococcus aureus (MSSA, meth- icillin-sensitive Staphylococcus aureus; MRSA methicillin-resistant Staphylococcus aureus), Escherichia coli, Streptococcus pneumoniae, Streptococcus pyogenes, and Pseudomonas aeruginosa as target organisms [1]. The 18-mer peptides as well as LL-37 inhibited the growth of these bacteria, and 18-mer LLKKK was the most potent among the peptide derivatives (Figure 5).

View Article: PubMed Central - PubMed

Show MeSH