NMR-Based Structural Characterization of a Two-Disulfide-Bonded Analogue of the FXIIIa Inhibitor Tridegin: New Insights into Structure–Activity Relationships

NMR-Based Structural Characterization of a Two-Disulfide-Bonded Analogue of the FXIIIa Inhibitor Tridegin: New Insights into Structure–Activity Relationships

The saliva of blood-sucking leeches contains a plethora of anticoagulant substances. One of these compounds derived from <i>Haementeria ghilianii</i>, the 66mer three-disulfide-bonded peptide tridegin, specifically inhibits the blood coagulation factor FXIIIa. Tridegin represents a poten...

Full description

Bibliographic Details
Main Authors: Thomas Schmitz, Ajay Abisheck Paul George, Britta Nubbemeyer, Charlotte A. Bäuml, Torsten Steinmetzer, Oliver Ohlenschläger, Arijit Biswas, Diana Imhof
Format: Article
Language:English
Published: MDPI AG 2021-01-01
Series:International Journal of Molecular Sciences
Subjects:
coagulation factor XIIIa
transglutaminase
coagulation cascade
tridegin
peptide inhibitor
cysteine-rich
Online Access:https://www.mdpi.com/1422-0067/22/2/880

Internet

https://www.mdpi.com/1422-0067/22/2/880

Similar Items