| Texto completo | |
| Autor(es): |
Torres-Obreque, Karin
;
Kleingesinds, Eduardo Krebs
;
Santos, Joao H. P. M.
;
Carretero, Gustavo
;
Rabelo, Jheniffer
;
Converti, Attilio
;
Monteiro, Gisele
;
Pessoa Jr, Adalberto
;
Rangel-Yagui, Carlota O.
Número total de Autores: 9
|
| Tipo de documento: | Artigo Científico |
| Fonte: | PREPARATIVE BIOCHEMISTRY & BIOTECHNOLOGY; v. N/A, p. 11-pg., 2023-09-11. |
| Resumo | |
Thermostability is an important and desired feature of therapeutic proteins and is critical for the success or failure of protein drugs development. It can be increased by PEGylation-binding of poly(ethylene glycol) moieties-or glycosylation-post-translational modification to add glycans. Here, the thermostability and thermodynamic parameters of native, PEGylated, and glycosylated versions of the antileukemic enzyme crisantaspase were investigated. First-order kinetics was found to describe the irreversible deactivation process. Activation energy of the enzyme-catalyzed reaction (E*) was estimated for native, PEGylated, and glycosylated enzyme (10.2, 14.8, and 18.8 kJ mol(-1) respectively). Half-life decreased progressively with increasing temperature, and lon-ger half-life was observed for PEG-crisantaspase (87.74 min) at 50 degrees C compared to the native form (9.79 min). The activation energy of denaturation of PEG-crisantaspase (307.1 kJ mol(-1)) was higher than for crisantaspase (218.1 kJ mol(-1)) and Glyco-crisantaspase (120.0 kJ mol(-1)), which means that more energy is required to overcome the energy barrier of the unfolding process. According to our results, PEG-crisantaspase is more thermostable than its native form, while Glyco-crisantaspase is more thermosensitive. (AU) | |
| Processo FAPESP: | 16/22065-5 - Pegilação N-terminal de proteínas e purificação por sistemas aquosos bifásicos |
| Beneficiário: | Carlota de Oliveira Rangel Yagui |
| Modalidade de apoio: | Auxílio à Pesquisa - Regular |
| Processo FAPESP: | 17/20384-9 - Desenvolvimento de processo de purificação de L-asparaginase humanizada e sua caracterização |
| Beneficiário: | Eduardo Krebs Kleingesinds |
| Modalidade de apoio: | Bolsas no Brasil - Doutorado |
| Processo FAPESP: | 13/08617-7 - Produção de L-asparaginase extracelular: da bioprospecção à engenharia de um biofármaco antileucêmico |
| Beneficiário: | Adalberto Pessoa Junior |
| Modalidade de apoio: | Auxílio à Pesquisa - Temático |
| Processo FAPESP: | 18/25994-2 - Desenvolvimento de novas plataformas de PEGuilação de proteínas com potencial terapêutico com recurso à microfluídica |
| Beneficiário: | João Henrique Picado Madalena Santos |
| Modalidade de apoio: | Bolsas no Brasil - Pós-Doutorado |