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1.
Indian J Dermatol Venereol Leprol ; 2008 Jan-Feb; 74(1): 32-4
Artigo em Inglês | IMSEAR | ID: sea-52980

RESUMO

BACKGROUND AND AIMS: Mycobacterium leprae is an obligate intracellular pathogen. Ligand-binding is an important factor in the success of chemoprevention and chemotherapy. A new drug that can inhibit M. leprae binding to and activation of, ErbB2 and Erk1/2 in primary Schwann cells is the new therapeutic option. However, the ligand-binding pattern of ErbB2 has never been clarified. METHODS: In this work, the author performed a ligand-binding prediction for ErbB2 using a new bioinformatics tool. RESULTS: According to this study, nine strong possible ligands can be identified. CONCLUSION: These sites can be useful for further drug-development studies.


Assuntos
Sítios de Ligação , Biologia Computacional , Desenho de Fármacos , Humanos , Hanseníase/metabolismo , Ligantes , Mycobacterium leprae/metabolismo , Valor Preditivo dos Testes , Ligação Proteica , Receptor ErbB-2/química , Virulência
2.
Yonsei Medical Journal ; : 58-64, 2003.
Artigo em Inglês | WPRIM | ID: wpr-186280

RESUMO

A humanized monoclonal antibody against HER2 has been using in a clinical setting and has been shown to possess therapeutic properties. A mimetic peptide against HER2 was also reported to bind to the HER2 receptor with some therapeutic potential. Based on a previous report and the sequence of Herceptin, we designed oligonucleotides of anti-HER2 mimetic peptides, named V2 and V3 peptides, in order to develop a peptide- producing vector system for biologic therapy against HER2- overexpressing cancers. We also adopted the sequence of a previously reported mimetic peptide, V1 (Park BW et al. Nat. Biotechnol, 2000, 18: 194-198), as a reference peptide. We examined the effects of the V2 and V3 peptides against the HER2-overexpressing cell lines, SK-BR-3 and T6-17. Transient transfection of the construct expressing V1 and V2 inhibited cell proliferation in HER2-overexpressing cell lines by 20 - 30%, but had no effect on the HER2-negative NIH3T3 cells. The proliferation inhibition shown by V2 was slightly better than that shown by V1. Recombinant peptides V2 and V3 were produced on a large scale in an E. coli system, and the V2 peptide showed anti-HER2-specific tumor cell proliferation inhibition of 10% to 30%. Current results suggest that anti-HER2 mimetic peptides, overexpressed by a constitutive promoter or produced in an E. coli system, could specifically inhibit the proliferation of HER2-expressing cancer cells. Further efforts to augment the biologic specificity and efficacy and to develop new technologies for the purification of the peptide from the E coli system are needed.


Assuntos
Animais , Camundongos , Sequência de Aminoácidos , Divisão Celular/efeitos dos fármacos , Linhagem Celular , Oligopeptídeos/síntese química , Fragmentos de Peptídeos/síntese química , Receptor ErbB-2/química , Proteínas Recombinantes/síntese química , Tecnologia Farmacêutica , Transfecção
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