Chemical zymogens for the protein cysteinome

Autor: Mireia Casanovas Montasell, Pere Monge, Sheiliza Carmali, Livia Mesquita Dias Loiola, Dante Guldbrandsen Andersen, Kaja Borup Løvschall, Ane Bretschneider Søgaard, Maria Merrild Kristensen, Jean Maurice Pütz, Alexander N. Zelikin

Publikováno v: Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)

Reversible on/off switches for enzyme activity are foundational in nature but are challenging to design using tools of synthetic chemistry. Here the authors design chemical zymogens amenable for activation via biomolecular interactions.

Externí odkaz: https://doaj.org/article/f86f49355a604cf09148fd650aea7473

Chemical zymogens for the protein cysteinome

Autor: Mireia Casanovas Montasell, Pere Monge, Sheiliza Carmali, Livia Mesquita Dias Loiola, Dante Guldbrandsen Andersen, Kaja Borup Løvschall, Ane Bretschneider Søgaard, Maria Merrild Kristensen, Jean Maurice Pütz, Alexander N. Zelikin

Publikováno v: Montasell, M C, Monge, P, Carmali, S, Loiola, L M D, Andersen, D G, Løvschall, K B, Søgaard, A B, Kristensen, M M, Pütz, J M & Zelikin, A N 2022, ' Chemical zymogens for the protein cysteinome ', Nature Communications, vol. 13, 4861 . https://doi.org/10.1038/s41467-022-32609-1
Montasell, M C, Monge, P, Carmali, S, Dias Loiola, L M, Andersen, D G, Løvschall, K B, Søgaard, A B, Kristensen, M M, Pütz, J M & Zelikin, A N 2022, ' Chemical zymogens for the protein cysteinome ', Nature Communications, vol. 13, no. 1, 4861 . https://doi.org/10.1038/s41467-022-32609-1

We present three classes of chemical zymogens established around the protein cysteinome. In each case, the cysteine thiol group was converted into a mixed disulfide: with a small molecule, a non-degradable polymer, or with a fast-depolymerizing fuse

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c4e65646886a13fea642fa1f735dc80
https://pubmed.ncbi.nlm.nih.gov/35982075