Coding

Part:BBa_K3582012

Designed by: Avadhoot Jadhav   Group: iGEM20_IISER-Pune-India   (2020-10-15)
Revision as of 11:22, 15 October 2020 by Avadhoot (Talk | contribs)


Inhibitory Peptide sequence 1 for CD36-PfEMP CIDRa Domain Interaction

This inhibitory peptide sequence is designed using the interacting regions of CD36 protein with the CIDRa Domain of the PfEMP1 protein. This is a mutant variant of the wild type interacting sequence of the CD36 protein. The following characteristic properties are observed in the inhibitory peptide sequence: 1]Interaction Energy: - 18.8211 2]Stability Value:4.544

  • Values are relative to wild type sequence.

This biobrick synthesizes the inhibitory peptide sequence that is believed to bind more efficiently as compared to the wild type sequence. The peptide sequence is built using saturated mutagenesis. In this particular mutant sequence, the last amino acid of the Wild type sequence-Serine(S) is replaced with methionine(M). As a result, an up-gradation in its interactive properties is observed that is thought to improve its binding strength.

Figure 1. DNA sequence of the inhibitory peptide sequence with its translation output.
Figure 1.Interacting regions of the PfEMP1 CIDRa domain and the inhibitory peptide sequence 1 shown here in protein ribbon model.



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]

References

  • 1] The structural basis for CD36 binding by the malaria parasite.

Fu-Lien Hsieh1, Louise Turner2, Jani Reddy Bolla3, Carol V. Robinson3, Thomas Lavstsen2 & Matthew K. Higgins1


[edit]
Categories
Parameters
None