Data/hora: 02/06/2024 04:31:55

Provedor de dados: | 56
País: | Brazil
Título: | The use of protein structure/activity relationships in the rational design of stable particulate delivery systems
Autores: | Costa,M.H.B.; Quintilio,W.; Sant'Anna,O.A.; Faljoni-Alário,A.; Araujo,P.S. de.
Data: | 2002-06-01
Ano: | 2002
Palavras-chave: | Protein stability; Hydrophobic modification; Vaccine delivery system; Drug delivery system; Adjuvant.
Resumo: | The recombinant heat shock protein (18 kDa-hsp) from Mycobacterium leprae was studied as a T-epitope model for vaccine development. We present a structural analysis of the stability of recombinant 18 kDa-hsp during different processing steps. Circular dichroism and ELISA were used to monitor protein structure after thermal stress, lyophilization and chemical modification. We observed that the 18 kDa-hsp is extremely resistant to a wide range of temperatures (60% of activity is retained at 80ºC for 20 min). N-Acylation increased its ordered structure by 4% and decreased its ß-T1 structure by 2%. ELISA demonstrated that the native conformation of the 18 kDa-hsp was preserved after hydrophobic modification by acylation. The recombinant 18 kDa-hsp resists to a wide range of temperatures and chemical modifications without loss of its main characteristic, which is to be a source of T epitopes. This resistance is probably directly related to its lack of organization at the level of tertiary and secondary structures.
Tipo: | Info:eu-repo/semantics/other
Idioma: | Inglês
Identificador: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2002000600014
Editor: | Associação Brasileira de Divulgação Científica
Relação: | 10.1590/S0100-879X2002000600014
Formato: | text/html
Fonte: | Brazilian Journal of Medical and Biological Research  v.35 n.6 2002
Fonte: | info:eu-repo/semantics/openAccess