Abstract
Tyrosine sulfation is an important post-translational modification of peptides and proteins which underpins and modulates many protein-protein interactions. In order to overcome the inherent instability of the native modification, we report the synthesis of two sulfonate analogues and their incorporation into two thrombin-inhibiting sulfopeptides. The effective mimicry of these sulfonate analogues for native sulfotyrosine was validated in the context of their thrombin inhibitory activity and binding mode, as determined by X-ray crystallography.
Original language | English |
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Pages (from-to) | 10923-10926 |
Number of pages | 4 |
Journal | Chemical Communications |
Volume | 57 |
Issue number | 83 |
DOIs | |
Publication status | Published - 19 Oct 2021 |
Externally published | Yes |
Keywords
- TYROSINE SULFATION
- ANTICOAGULANT
- SULFOPEPTIDES
- SULFOPROTEINS
- RECOGNITION
- REVEALS
- BINDING
- SALIVA