Abstract
Casein has been recognized as a good source of bioactive peptides that can be used for the production of functional food. In this study, thrombin inhibitory peptides from casein were screened by bioinformatics based on sequences predicted from in silico enzymatic digestion with trypsin, and identified by UPLC-Q-TOF-MS/MS with Mascot analysis. Molecular docking was conducted using the software of Discovery Studio 2017 to provide the potential mechanism underlying the thrombin inhibitory activity of the peptides. A total of 35 novel peptides with thrombin inhibitory activity were identified. Moreover, FQSEEQQQTEDELQDK, derived from beta-casein (fragment 33–48), showed a remarkable sequence similarity with fragment 54–65 of hirudin, and exhibited strong inhibitory activity against thrombin. FQSEEQQQTEDELQDK had similar target domain (Lys36-Gln38-Arg73-Thr74-Lys81-Ile82-Lys110) on the stereo structure of thrombin compared with hirudin. This domain belongs to the partial structure of the active site 2 of thrombin (PDB: 2BVR), and it also located at the exosite I motif buried in the external surface of thrombin molecule, with potential inhibitory activity of the peptide.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
