Difference between revisions of "Part:BBa K3561004"

Revision as of 13:55, 9 October 2020

W3W4A6C11

This peptide is expected to be a palladium reducing peptide. This peptide is modified by our team from the palladium binding peptide A6C11 (Coppage et al., 2013). We have incorporated a tryptophan residue into the peptide as it was reported that tryptophan is capable of reducing palladium (Chiu et al., 2010). We chose a double tryptophan structure at residues 3 and 4 as it was said that a double tryptophan is more effective than a single tryptophan structure in gold(Tan et al., 2010). We would like to investigate whether a double tryptophan will be more effective in palladium. We would also like to investigate what effects will there have if we inserted the tryptophan residue at different positions.

This peptide has an isoelectric point of 9.0, a molecular weight of 1.43 kDa and hydrophobicity of 37.71. 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 serine and threonine residues at position 2 and 10 are also reported to be important in binding with palladium(Sarikaya et al., 2003). The amino acid sequence of the peptide is TSWWVAPTLRCL.

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/.

Chiu, et al. Size-Controlled Synthesis of Pd Nanocrystals Using a Specific Multifunctional Peptide. 2010, pubmed.ncbi.nlm.nih.gov/20648291/.

DI;, Tan YN;Lee JY;Wang. Uncovering the Design Rules for Peptide Synthesis of Metal Nanoparticles. 2010, pubmed.ncbi.nlm.nih.gov/20355728/. 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]

@@ Line 3: / Line 3: @@
 <partinfo>BBa_K3561004 short</partinfo>
-This peptide is expected to be a palladium reducing peptide. This peptide is modified by our team from the palladium binding peptide A6C11 (Coppage et al., 2013). We have incorporated a tryptophan residue into the peptide as it was reported that tryptophan is capable of reducing palladium (Chiu et al., 2010). We chose a double tryptophan structure at residues 3 and 4 as it was said that a double tryptophan is more effective than a single tryptophan structure in gold(Tan et al., 2010). We would like to investigate whether a double tryptophan will be more effective in palladium. We would also like to investigate what effects will there have if we inserted the tryptophan residue at different positions. This peptide has an isoelectric point of 9.0, a molecular weight of 1.43 kDa and hydrophobicity of 37.71. 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 serine and threonine residues at position 2 and 10 are also reported to be important in binding with palladium(Sarikaya et al., 2003). The amino acid sequence of the peptide is TSWWVAPTLRCL.
+This peptide is expected to be a palladium reducing peptide. This peptide is modified by our team from the palladium binding peptide A6C11 (Coppage et al., 2013). We have incorporated a tryptophan residue into the peptide as it was reported that tryptophan is capable of reducing palladium (Chiu et al., 2010). We chose a double tryptophan structure at residues 3 and 4 as it was said that a double tryptophan is more effective than a single tryptophan structure in gold(Tan et al., 2010). We would like to investigate whether a double tryptophan will be more effective in palladium. We would also like to investigate what effects will there have if we inserted the tryptophan residue at different positions.
+This peptide has an isoelectric point of 9.0, a molecular weight of 1.43 kDa and hydrophobicity of 37.71. 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 serine and threonine residues at position 2 and 10 are also reported to be important in binding with palladium(Sarikaya et al., 2003). The amino acid sequence of the peptide is TSWWVAPTLRCL.
 <h2>References</h2>