Difference between revisions of "Part:BBa K3561002"

Revision as of 13:51, 21 October 2020

A6C11(Coppage et al., 2013)

A6C11 is a palladium binding peptide. It is used as a library peptide in our project to act as a template for our mutations. The results of molecular dynamics for our modified peptides are also compared with this peptide. This peptide has an isoelectric point of 9.0, a molecular weight of 1.25kDa and hydrophobicity of 24.06. The alanine residue at position 6 has a minimal binding with palladium while the cysteine residue at position 11 has a strong binding with palladium, it was suggested that this may have higher efficiency(Coppage et al., 2013). The arginine residue at position 10 is reported to coordinate with palladium(Pacardo et al., 2009). The serine and threonine residues at positions 1 and 2 are also reported to be important in binding with palladium(Sarikaya et al., 2003). The amino acid sequence TSNAVAPTLRCL.

References

Pacardo, et al. “Biomimetic Synthesis of Pd Nanocatalysts for the Stille Coupling Reaction.” ACS Nano, U.S. National Library of Medicine, 2009, pubmed.ncbi.nlm.nih.gov/19422199/.

Sarikaya et al. “Molecular Biomimetics: Nanotechnology through Biology.” Nature News, Nature Publishing Group, 2003, www.nature.com/articles/nmat964.

Coppage, et al. “Exploiting Localized Surface Binding Effects to Enhance the Catalytic Reactivity of Peptide-Capped Nanoparticles.” Journal of the American Chemical Society, U.S. National Library of Medicine, 2013, pubmed.ncbi.nlm.nih.gov/23865951/.

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]

Modelling

From our molecular dynamics, we were able to determine the distance of the peptide from the palladium ion, the radius of gyration, the RMSD score and the total energy of the system.

We can compare the bond lengths of our peptides with the distances reported by previous literature to evaluate the attraction between the palladium ion and the peptide. The distance should also stay consistent.

The radius of gyration represent the compactness of the peptide, the peptide is generally more stable if the standard deviation is smaller. RMSD measures the average distance each atom deviated from the start of the simulation. A small deviation in RMSD indicates a stable structure.

We have also evaluated the total energy of the system during the simulation, if the total energy of the system varies a lot, it indicates that the law of energy conservation has not been fulfilled and further in vitro analysis is required to prove its reducing ability.

More details of how our molecular dynamics is run can be found on our team wiki.

800px

@@ Line 18: / Line 18: @@
 <span class='h3bb'>Sequence and Features</span>
 <partinfo>BBa_K3561002 SequenceAndFeatures</partinfo>
+<h2>Modelling</h2>
+From our molecular dynamics, we were able to determine the distance of the peptide from the palladium ion, the radius of gyration, the RMSD score and the total energy of the system.
+We can compare the bond lengths of our peptides with the distances reported by previous literature to evaluate the attraction between the palladium ion and the peptide. The distance should also stay consistent.
+The radius of gyration represent the compactness of the peptide, the peptide is generally more stable if the standard deviation is smaller. RMSD measures the average distance each atom deviated from the start of the simulation. A small deviation in RMSD indicates a stable structure.
+We have also evaluated the total energy of the system during the simulation, if the total energy of the system varies a lot, it indicates that the law of energy conservation has not been fulfilled and further in vitro analysis is required to prove its reducing ability.
+More details of how our molecular dynamics is run can be found on our team wiki.
+[[File:BBa K3561002 radius of gyration 2.jpeg|800px]]
+[[File:BBa K3561002 potential 2.jpg|800px]]
+[[File:BBa K3561002 RMSD 2.jpg|800px]]
+[[File:BBa K3561002 total energy 2.jpg|800px]]