In silico approach of modified melanoma peptides and their immunotherapeutic potential
| Autor: | J. I. N. Oliveira, Umberto L. Fulco, J. L. S. Santos, A. C. L. Pereira, Valder N. Freire, Katyanna S Bezerra |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences Chemistry Immunogenicity In silico Melanoma General Physics and Astronomy Peptide Computational biology medicine.disease Glycoprotein 100 03 medical and health sciences 0302 clinical medicine Immune system Antigen 030220 oncology & carcinogenesis medicine Physical and Theoretical Chemistry Binding site 030304 developmental biology |
| Zdroj: | Physical Chemistry Chemical Physics. 23:2836-2845 |
| ISSN: | 1463-9084 1463-9076 |
| DOI: | 10.1039/d0cp05322h |
| Popis: | Melanoma is a type of skin cancer with increasing incidence worldwide and high lethality. Conventional forms of treatment are not effective in advanced cancer stages. Hence, immunotherapeutic approaches have been tested to modulate immune response against tumor cells. Some vaccine models using tumor-associated antigens (TAAs) such as glycoprotein 100 (gp100) have been studied, but their expected effectiveness has not been shown until now. Antigen immunogenicity is a crucial point to improve the immune response, and therefore mutations are inserted in peptide sequences. It is possible to understand the interactions which occur between peptides and immune system molecules through computer simulation, and this is essential in order to guide efficient vaccine models. In this work, we have calculated the interaction binding energies of crystallographic data based on modified gp100 peptides and HLA-A*0201 using density functional theory (DFT) and the molecular fractionation with conjugated caps (MFCC) approach. Our results show the most relevant residue-residue interactions, the impact of three mutations in their binding sites, and the main HLA-A*0201 amino acids for peptide–HLA binding. |
| Databáze: | OpenAIRE |
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