Difference between revisions of "Part:BBa K1835502"

Latest revision as of 22:53, 18 September 2015

Cysteine-Deleted Protegrin I

Cysteine-deleted Protegrin (CDP) contains the same sequence as Protegrin-1 minus the four cysteine residues. CDP’s lack of cysteine residues means it cannot form disulfide bridges to bring together the permanent beta-sheet secondary structure. Although the secondary structure is no longer permanent with the deletion of the cysteines, it can still be achieved transiently and maintained if it experiences the correct interactions. CDP is still capable of killing bacteria, which are the original intended target of these peptides and thus show a greater degree of binding specificity and affinity. In BioBrick form, the haemolytic inactivity has not yet been verified.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
INCOMPATIBLE WITH RFC[12]
Illegal NotI site found at 8
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_K1835502 short</partinfo>
-Functionally similar to BBa_K628000, but with two cysteine-cysteine disulfide bridges removed. It is reported that this change does not lower anti-microbial activity but greatly reduced haemolytic effect.
+Cysteine-deleted Protegrin (CDP) contains the same sequence as Protegrin-1 minus the four cysteine residues. CDP’s lack of cysteine residues means it cannot form disulfide bridges to bring together the permanent beta-sheet secondary structure. Although the secondary structure is no longer permanent with the deletion of the cysteines, it can still be achieved transiently and maintained if it experiences the correct interactions. CDP is still capable of killing bacteria, which are the original intended target of these peptides and thus show a greater degree of binding specificity and affinity. In BioBrick form, the haemolytic inactivity has not yet been verified.
 <!-- Add more about the biology of this part here