Difference between revisions of "Part:BBa K3582027"

Revision as of 08:55, 24 October 2020

Inhibitory sequence 2 for PfEMP1-ICAM1 interaction

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

• 1] Interaction energy: -11.04 kcal/mol
• 2] Stability value: 6.08285 dG units
• 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. It is 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

References

• [1]Structure-Guided Identification of a Family of Dual Receptor-Binding PfEMP1 that Is Associated with Cerebral Malaria. (2017, March 8). PubMed Central (PMC). https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5374107/