Difference between revisions of "Part:BBa K1162008"

Latest revision as of 03:58, 28 September 2013

OH-CATH (3-34) antimicrobial peptide from the King Cobra (Ophiophagus hannah)

OH-CATH(3-34) is an antimicrobial peptide isolated and characterized from the king cobra (Ophiophagus hannah)(Zhao et al 2008). A member of the cathelicidin family, OH-CATH Cathelicidins in general have been well characterized and are known to have a diverse C-terminal antimicrobial domain connected to a conserved cathelin-like N-terminal domain (Nizet et al 2003). Specifically, OH-CATH has been studied for its toxicity against a wide range of gram negative and gram positive bacteria. OH-CATH has also been characterized for its potent activity against multi-drug resistant bacterial strains including MRSA (Li et al 2012). Further studies by (Zhang et al 2010) have shown that removing the first few amino acid residues of the peptide dramatically reduced the hemolytic activity while having only minute effects on antimicrobial properties. This attribute would be highly desirable in any usage that would interact with humans and helped to determine our choice our peptides. The combination of high bacterial toxicity with low hemolytic activity justify more testing into the precise mechanisms of OH-CATH and its ability to be used as a scaffold for other antibiotic purposes.

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]

@@ Line 1: / Line 1: @@
 __NOTOC__
 <partinfo>BBa_K1162008 short</partinfo>
-An antimicrobial peptide from the Cathelicidin family of peptides, isolated from the King Cobra (Ophiophagus hannah). Shortened version of the full 34 amino acid protein (C-terminal KR residues removed) that retains antibacterial properties while significantly removing hemolytic activity.
+OH-CATH(3-34) is an antimicrobial peptide isolated and characterized from the king cobra (Ophiophagus hannah)(Zhao et al 2008). A member of the cathelicidin family, OH-CATH Cathelicidins in general have been well characterized and are known to have a diverse C-terminal antimicrobial domain connected to a conserved cathelin-like N-terminal domain (Nizet et al 2003). Specifically, OH-CATH has been studied for its toxicity against a wide range of gram negative and gram positive bacteria. OH-CATH has also been characterized for its potent activity against multi-drug resistant bacterial strains including MRSA (Li et al 2012). Further studies by (Zhang et al 2010) have shown that removing the first few amino acid residues of the peptide dramatically reduced the hemolytic activity while having only minute effects on antimicrobial properties. This attribute would be highly desirable in any usage that would interact with humans and helped to determine our choice our peptides. The combination of high bacterial toxicity with low hemolytic activity justify more testing into the precise mechanisms of OH-CATH and its ability to be used as a scaffold for other antibiotic purposes.
 <!-- Add more about the biology of this part here