Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 3 de 3
Filtrar
Mais filtros












Base de dados
Tipo de estudo
Intervalo de ano de publicação
1.
Curr Drug Discov Technol ; 16(3): 285-289, 2019.
Artigo em Inglês | MEDLINE | ID: mdl-29793409

RESUMO

BACKGROUND: Anti-ovarian cancer vaccines based on minimal immune determinants uniquely expressed in ovarian cancer biomarkers appear to promise a high level of sensitivity and specificity for ovarian cancer immunodiagnostics, immunoprevention, and immunotherapy. METHODS: Using the Pir Peptide Match program, three ovarian cancer biomarkers - namely, sperm surface protein Sp17, WAP four-disulfide core domain protein 2, and müllerian-inhibiting substance - were searched for unique peptide segments not shared with other human proteins. Then, the unique peptide segments were assembled to define oligopeptides potentially usable as synthetic ovarian cancer antigens. RESULTS AND CONCLUSION: This study describes a methodology for constructing ovarian cancer biomarkerderived oligopeptide constructs that might induce powerful, specific, and non-crossreactive immune responses against ovarian cancer.


Assuntos
Hormônio Antimülleriano/química , Antígenos de Neoplasias/química , Biomarcadores Tumorais/química , Proteínas de Ligação a Calmodulina/química , Proteínas de Membrana/química , Neoplasias Ovarianas , Proteína 2 do Domínio Central WAP de Quatro Dissulfetos/química , Feminino , Humanos , Imunoterapia , Oligopeptídeos/uso terapêutico , Neoplasias Ovarianas/terapia
2.
Oral Implantol (Rome) ; 9(2): 83-88, 2016.
Artigo em Inglês | MEDLINE | ID: mdl-28042435

RESUMO

PURPOSE: To identify potential antigenic targets for Porphyromonas gingivalis vaccine development. MATERIALS AND METHODS: In the present study, we analyzed the Porphyromonas gingivalis, fimA type II primary amino acid sequence and characterized the similarity to the human proteome at the pentapeptide level. RESULTS: We found that exact peptide-peptide profiling of the fimbrial antigen versus the human proteome shows that only 19 out of 344 fimA type II pentapeptides are uniquely owned by the bacterial protein. CONCLUSIONS: The concept that protein immunogenicity is allocated in rare peptide sequences and the search the Porphyromonas gingivalis fimA type II sequence for peptides unique to the bacterial protein and absent in the human host, might be used in new therapeutical approaches as a significant adjunct to current periodontal therapies.

3.
Vaccines (Basel) ; 3(1): 74-89, 2015 Feb 05.
Artigo em Inglês | MEDLINE | ID: mdl-26344947

RESUMO

Epstein-Barr virus (EBV) infects B-, T-, and NK cells and has been associated not only with a wide range of lymphoid malignancies but also with autoimmune diseases such as lupus erythematosus, rheumatoid arthritis and, in particular, multiple sclerosis. Hence, effective immunotherapeutic approaches to eradicate EBV infection might overthrow cancer and autoimmunity incidence. However, currently no effective anti-EBV immunotherapy is available. Here we use the concept that protein immunogenicity is allocated in rare peptide sequences and search the Epstein-Barr nuclear antigen 1 (EBNA1) sequence for peptides unique to the viral protein and absent in the human host. We report on a set of unique EBV EBNA1 peptides that might be used in designing peptide-based therapies able to specifically hitting the virus or neutralizing pathogenic autoantibodies.

SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA
...