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Team:TU-Delft/PeptideResistance
From 2013.igem.org
Peptide Resistance
Proteolytic cleavage is the process of breaking the peptide bonds between amino acids in proteins. This process is carried out by enzymes called peptidases, proteases or proteolytic cleavage enzymes. We decided to perform a bioinformatic's analysis in order to investigate the existence of proteases that cleave our peptides in S.aureus organism. In that way, we can assure about the effectiveness of the peptides and give an estimation about being probable or not for the S.aureus to get resistant to the peptides.
In order to manage this, we performed a number of steps:
- The cleavage sites of the peptides were found.
- The proteases that cleave in the specific sites were also identified.
- The existence of the specific or similar proteases in S. aureus was investigated.
- Similarity in catalytic sites was taken into consideration
Results
The results obtained by our analysis are presented underneath.Magainin: GIGKYLHSAKKFGKAWVGEIMNS
| Protease | #cleavages | Position of Cleavage sites | Similarity found in S.aureus |
| Asp-N endopeptidase | 1 | 18 | No |
| Glutamyl endopeptidase | 1 | 19 | glutamyl endopeptidase [Staphylococcus aureus] ref|WP_000676526.1| |
| Pepsin A-1 | 2 | 5 11 | cathepsin E (EC 3.4.23.34) - Staphylococcus aureus (fragments) Similarity in segments but containing the catalytic site. |
| Chymotrypsin-high specificity | 3 | 5 12 16 | Segments of Similarity were found but on in the catalytic site |
Maximim-H5: ILGPVLGLVSDTLDDVLGIL
| Protease | #cleavages | Position of Cleavage sites | Similarity found in S.aureus |
| Asp-N endopeptidase | 3 | 10 13 14 | No |
Signiferin 2.1 IIGHLIKTALGMLGL
| Protease | #cleavages | Position of Cleavage sites | Similarity found in S.aureus |
| Trypsin | 1 | 7 | tyrosyl-tRNA synthetase [Staphylococcus aureus subsp. aureus ED133] ref|YP_005737201.1| similarity contained in the active site |
| LysC | 1 | 7 | No |
| Peptidyl-Lys metalloendopeptidase | 1 | 6 | No |
