Journal
STRUCTURE
Volume 25, Issue 4, Pages 655-+Publisher
CELL PRESS
DOI: 10.1016/j.str.2017.02.009
Keywords
-
Funding
- University of Padova, Italy
- University of Padova, Italy (UNIPD, Progetto Giovani Studiosi) [79122]
- University of Padova, Italy (UNIPD, Assegno di Ricerca) [11-2016]
Ask authors/readers for more resources
Peptides have gained increased interest as therapeutic agents during recent years. The high specificity and relatively low toxicity of peptide drugs derive from their extremely tight binding to their targets. Indeed, understanding the molecular mechanism of protein-peptide recognition has important implications in the fields of biology, medicine, and pharmaceutical sciences. Even if crystallography and nuclear magnetic resonance are offering valuable atomic insights into the assembling of the protein-peptide complexes, the mechanism of their recognition and binding events remains largely unclear. In this work we report, for the first time, the use of a supervised molecular dynamics approach to explore the possible protein-peptide binding pathways within a timescale reduced up to three orders of magnitude compared with classical molecular dynamics. The better and faster understating of the protein-peptide recognition pathways could be very beneficial in enlarging the applicability of peptide-based drug design approaches in several biotechnological and pharmaceutical fields.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available