U-SPY | Artificial metalloenzymes Using SPY protein

Summary
Protein redesign allows to devise enzymes with new structure and functions, however, the introduction of artificial metal cofactors to a protein and tailoring the second coordination sphere of the metal centre remains challenging. SPY technology is a way to tackle these problems.
In U-SPY this technology will be used to devise new artificial metalloenzymes capable for photostimulated reactions. This tagging system has been widely used but no examples are reported about SPY-based metalloenzymes. The SPY proteins will be obtained by the fusion of the SpyCatcher protein and the metalated SpyTag peptides containing copper and ruthenium metal centres.
The computational design of the SPY systems will be followed by the synthesis, covalent modification and metalation of peptides (SpyTags). By the fusion of the various SpyTags and SpyCathers a library of SPY-based metalloenzymes will be developed, characterized and tested as catalysts for photostimulated reactions including atom transfer radical addition and isomerization reactions.
This fellowship will give the opportunity to the candidate to spend 24 months in the University of Parma, under the supervision of Prof. Tegoni, who has a proven track record in the multidisciplinary field of bioinorganic and coordination chemistry, peptide design and photocatalysis.
One of the project main expected results will be to prove the suitability of SPY technology for devising artificial metalloenzymes and the possibility to use these biocatalysts in the industry. The implementation of the project will exploit the researcher’s synthetic skills and will give him the chance to be an independent researcher in the future. It will also give the possibility to integrate him in the academic system by a tenure track position after the fellowship.
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More information & hyperlinks
Web resources: https://cordis.europa.eu/project/id/101152452
Start date: 01-10-2024
End date: 30-09-2026
Total budget - Public funding: - 188 590,00 Euro
Cordis data

Original description

Protein redesign allows to devise enzymes with new structure and functions, however, the introduction of artificial metal cofactors to a protein and tailoring the second coordination sphere of the metal centre remains challenging. SPY technology is a way to tackle these problems.
In U-SPY this technology will be used to devise new artificial metalloenzymes capable for photostimulated reactions. This tagging system has been widely used but no examples are reported about SPY-based metalloenzymes. The SPY proteins will be obtained by the fusion of the SpyCatcher protein and the metalated SpyTag peptides containing copper and ruthenium metal centres.
The computational design of the SPY systems will be followed by the synthesis, covalent modification and metalation of peptides (SpyTags). By the fusion of the various SpyTags and SpyCathers a library of SPY-based metalloenzymes will be developed, characterized and tested as catalysts for photostimulated reactions including atom transfer radical addition and isomerization reactions.
This fellowship will give the opportunity to the candidate to spend 24 months in the University of Parma, under the supervision of Prof. Tegoni, who has a proven track record in the multidisciplinary field of bioinorganic and coordination chemistry, peptide design and photocatalysis.
One of the project main expected results will be to prove the suitability of SPY technology for devising artificial metalloenzymes and the possibility to use these biocatalysts in the industry. The implementation of the project will exploit the researcher’s synthetic skills and will give him the chance to be an independent researcher in the future. It will also give the possibility to integrate him in the academic system by a tenure track position after the fellowship.

Status

SIGNED

Call topic

HORIZON-MSCA-2023-PF-01-01

Update Date

22-11-2024
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Horizon Europe
HORIZON.1 Excellent Science
HORIZON.1.2 Marie Skłodowska-Curie Actions (MSCA)
HORIZON.1.2.0 Cross-cutting call topics
HORIZON-MSCA-2023-PF-01
HORIZON-MSCA-2023-PF-01-01 MSCA Postdoctoral Fellowships 2023