Difference between revisions of "Part:BBa K3582027"
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*1] Interaction energy: -9.69483 kcal/mol | *1] Interaction energy: -9.69483 kcal/mol | ||
*2] Stability value: 4.33159 dG units | *2] Stability value: 4.33159 dG units | ||
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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] | 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] | ||
Latest revision as of 07:53, 26 October 2020
Inhibitory sequence 2 for PfEMP1-ICAM1 interaction
The following characteristic properties are observed in this inhibitory peptide sequence:
- 1] Interaction energy: -9.69483 kcal/mol
- 2] Stability value: 4.33159 dG units
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
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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/