Data/hora: 02/06/2024 11:40:07

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