Part:BBa_K4200313:Design
Antimicrobial Peptide to inhibit Multivalent Adhesion Molecule 7 (MAM7)
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
Each of Fibronectin's five repeats of the type I module was considered to be a potential antimicrobial peptide. Each of these peptides was then separately docked with MAM7. Peptide number 5, which had the highest score was taken, for which multiple modification cycles involving conserved and nonconserved mutations were conducted to yield the Antimicrobial Peptide with the best binding affinity to MAM7.
The peptide will be produced using the pET-22b(+) vector system and Escherichia coli BL21 as our chassis.
Source
The sequence for the antimicrobial peptide is derived from Trout Fibronectin
References
A. M. Krachler and K. Orth, “Functional characterization of the interaction between bacterial adhesin Multivalent Adhesion Molecule 7 (MAM7) protein and its host cell ligands,” J. Biol. Chem., vol. 286, no. 45, pp. 38939–38947, Nov. 2011, doi: 10.1074/JBC.M111.291377.
J.-H. Ong, W.-L. Wong, F.-C. Wong, and T.-T. Chai, “Targeting PirAvp and PirBvp Toxins of Vibrio parahaemolyticus with Oilseed Peptides: An In Silico Approach,” Antibiotics, vol. 10, no. 10, p. 1211, Oct. 2021, doi: 10.3390/antibiotics10101211.