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Grant: Idea to Innovation

University of Windsor

$125,000.00

I2I Phase 1a: Development of thermally-sensitive protected cysteine residues for controlled disulfide bond formation

EF 2021-22

Résumé
This project supports an emerging technology developed by the Trant Lab at the University of Windsor to help researchers and pharmaceutical companies make a subclass of drugs and research tools far more easily than current methods. Peptides, short chains of amino acids, and conceptually short proteins, are often excellent drug candidates or probes for researchers to better understand biology and to treat disease. Like for all molecules, form is function, and peptides adopt specific conformations both through the inherent twists programmed into the amino acid sequence, but also through cross-links between different parts of the peptides through cysteine residues. Cysteine has a sulfur on it, and this allows it to make a bond to another sulfur atom on another cysteine amino acid, providing shape to the resulting drug. This is relatively simple when only one of these disulfide bonds is present, but becomes increasingly complex as more are introduced, meaning that any research team needs to have specialist peptide organic chemists to design and troubleshoot the approach. Furthermore, forming the bonds selectively means that the many different chemical steps are needed, often with purification in between each step greatly increasing costs. We have a simple general solution that uses heat as the only trigger to make these materials. This component of the project will support our reduction-to-practice where we apply our approach to more and more peptide examples to secure the interest of industrial partners, both for those that are using it directly for a specific project (Cotinga), and for fine chemical companies (Sigma-Aldrich) that would look to market the technology as a "kit." These will continue to be made here in Canada and sold worldwide to benefit the Windsor, Ontario, and Canadian economy and biotech industry.
Programme
Idea to Innovation
Bénéficiaire
Emplacement
Ontario, Canada
Type de bénéficiaire
Academia
Type
Grant
Source
NSERC's Awards Data

Tel que publié

Application id
561575-2021
Name nom
Trant, John
Department département
Chemistry and Biochemistry
Organization id
37
Institution établissement
University of Windsor
Province en
Ontario
Province fr
Ontario
Country en
CANADA
Country fr
CANADA
Fiscal year exercice financier
2021
Competition year année de concours
2021
Award amount
125000
Program id
I2IPJ
Program name en
Idea to Innovation
Program name fr
De l'idée à l'innovation
Group en
Research partnerships programs
Group fr
Programmes de partenariat
Committee code
96
Committee name en
RPP Internal Decision Cttee
Committee name fr
Cté de décision interne - PPR
Area of application code
504
Area of application group en
Manufacturing processes and products
Area of application group fr
Procédés et produits industriels
Area of application en
Human pharmaceuticals
Area of application fr
Produits pharmaceutiques administrables à l'homme
Research subject code
3705
Research subject group en
Organic chemistry
Research subject group fr
Chimie organique
Research subject en
Bio-organic chemistry
Research subject fr
Chimie bio-organique
Installment
inst:1
Partie
1
Nb partie
1
Application title
I2I Phase 1a: Development of thermally-sensitive protected cysteine residues for controlled disulfide bond formation
Keyword
NSERC
Application summary
This project supports an emerging technology developed by the Trant Lab at the University of Windsor to help researchers and pharmaceutical companies make a subclass of drugs and research tools far more easily than current methods. Peptides, short chains of amino acids, and conceptually short proteins, are often excellent drug candidates or probes for researchers to better understand biology and to treat disease. Like for all molecules, form is function, and peptides adopt specific conformations both through the inherent twists programmed into the amino acid sequence, but also through cross-links between different parts of the peptides through cysteine residues. Cysteine has a sulfur on it, and this allows it to make a bond to another sulfur atom on another cysteine amino acid, providing shape to the resulting drug. This is relatively simple when only one of these disulfide bonds is present, but becomes increasingly complex as more are introduced, meaning that any research team needs to have specialist peptide organic chemists to design and troubleshoot the approach. Furthermore, forming the bonds selectively means that the many different chemical steps are needed, often with purification in between each step greatly increasing costs. We have a simple general solution that uses heat as the only trigger to make these materials. This component of the project will support our reduction-to-practice where we apply our approach to more and more peptide examples to secure the interest of industrial partners, both for those that are using it directly for a specific project (Cotinga), and for fine chemical companies (Sigma-Aldrich) that would look to market the technology as a "kit." These will continue to be made here in Canada and sold worldwide to benefit the Windsor, Ontario, and Canadian economy and biotech industry.