Difference between revisions of "Part:BBa K3582024"

Revision as of 16:12, 20 October 2020

Inhibitory Sequence 1 for PfEMP-1 and ICAM-1 interaction

The following characteristic properties are observed in this inhibitory peptide sequence:

1] Interaction energy: -11.04
2] Stability value: 6.08285
These values are relative to the wild type sequence

This biobrick is able to synthesize the inhibitory peptide which is believed to be able to bind more effectively to PfEMP1 as compared to the wild type sequence. The peptide sequence is designed using saturation mutagenesis. Many residues were mutated and it is thought that this change can confer extra stability to the inhibitory peptide as it binds to the parasite protein. These inhibitors form hydrogen bonds with the PfEMP1 protein to stop PfEMP1’s interaction with ICAM-1. They are rich in Glycine and Proline residues and it has been documented that GP- rich residues bind strongly to the DBL-beta domain of PfEMP1A.[1]

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 7: / Line 7: @@
 *2] Stability value: 6.08285
 *These values are relative to the wild type sequence
-This biobrick is able to synthesize the inhibitory peptide which is believed to be able to bind more effectively to PfEMP1 as compared to the wild type sequence. The peptide sequence is designed using saturation mutagenesis. Many residues were mutated and it is thought that this change can confer extra stability to the inhibitory peptide as it binds to the parasite protein.  These inhibitors form hydrogen bonds with the PfEMP1 protein to stop PfEMP1’s interaction with ICAM-1.
+This biobrick is able to synthesize the inhibitory peptide which is believed to be able to bind more effectively to PfEMP1 as compared to the wild type sequence. The peptide sequence is designed using saturation mutagenesis. Many residues were mutated and it is thought that this change can confer extra stability to the inhibitory peptide as it binds to the parasite protein.  These inhibitors form hydrogen bonds with the PfEMP1 protein to stop PfEMP1’s interaction with ICAM-1. They are rich in Glycine and Proline residues and it has been documented that GP- rich residues bind strongly to the DBL-beta domain of PfEMP1A.[1]