Team:TU-Delft/NovelPeptides

From 2013.igem.org

(Difference between revisions)
Line 8: Line 8:
<html>
<html>
 +
<p align="justify">
 +
The antimicrobial peptide(AMPs) field is growing rapidly in response to the demand
 +
for novel antimicrobial agents. In particular AMPs are promising candidates
 +
in the fight against antibiotic-resistant pathogents due to their low toxicity,
 +
and broad range of activity. Antimicrobial peptides are generally between 12 and 50 amino acids long. These peptides
 +
include two or more positively charged residues provided by arginine, lysine
 +
or, in acidic environments, histidine, and a large proportion of hydrophobic residues.
 +
</p>
 +
<p align="justify">
 +
Due to the fact that AMPs constitute a current research area, both the
 +
knowledge and the experimentally validated data are rapidly increasing.It
 +
was decided to use these data in order to create novel peptides which will
 +
be high toxic for S.aureus but low toxic for E.coli. The method that was
 +
developed is described in the following sections.
 +
 +
</p>
</html>
</html>

Revision as of 08:36, 11 September 2013

Novel Peptides

The antimicrobial peptide(AMPs) field is growing rapidly in response to the demand for novel antimicrobial agents. In particular AMPs are promising candidates in the fight against antibiotic-resistant pathogents due to their low toxicity, and broad range of activity. Antimicrobial peptides are generally between 12 and 50 amino acids long. These peptides include two or more positively charged residues provided by arginine, lysine or, in acidic environments, histidine, and a large proportion of hydrophobic residues.

Due to the fact that AMPs constitute a current research area, both the knowledge and the experimentally validated data are rapidly increasing.It was decided to use these data in order to create novel peptides which will be high toxic for S.aureus but low toxic for E.coli. The method that was developed is described in the following sections.