@article{10336/23651,
author = {González R.},
author = {Suárez C.F.},
author = {Bohórquez H.J.},
author = {Patarroyo M.A.},
author = {Patarroyo M.E.},
year = {2017},
url = {https://repository.urosario.edu.co/handle/10336/23651},
abstract = {Peptide presentation by the major histocompatibility complex (MHC) is a key process for triggering a specific immune response. Studying peptide-MHC (pMHC) binding from a structural-based approach has potential for reducing the costs of investigation into vaccine development. This study involved using two semi-empirical quantum chemistry methods (PM7 and FMO-DFTB) for computing the binding energies of peptides bonded to HLA-DR1 and HLA-DR2. We found that key stabilising water molecules involved in the peptide binding mechanism were required for finding high correlation with IC50 experimental values. Our proposal is computationally non-intensive, and is a reliable alternative for studying pMHC binding interactions. © 2016 Elsevier B.V.},
booktitle = {Chemical Physics Letters, ISSN:92614, Vol.668,(2017); pp. 29-34},
title = {Semi-empirical quantum evaluation of peptide – MHC class II binding},
publisher = {Elsevier B.V.},
keywords = {Bins},
keywords = {Molecules},
keywords = {Peptides},
keywords = {Quantum chemistry},
keywords = {Binding interaction},
keywords = {Experimental values},
keywords = {FMO-DFTB},
keywords = {HLA-DR},
keywords = {Major histocompatibility complex},
keywords = {Quantum chemistry methods},
keywords = {Receptor-ligand interactions},
keywords = {Vaccine development},
keywords = {Binding energy},
keywords = {FMO-DFTB},
keywords = {HLA-DR},
keywords = {PM7},
keywords = {Receptor-ligand interactions},
doi = {https://doi.org/10.1016/j.cplett.2016.12.015},
}