The use of protein structure/activity relationships in the rational design of stable particulate delivery systems
Braz. j. med. biol. res
;
35(6): 727-730, June 2002. ilus, tab
Artigo
em Inglês
| LILACS
| ID: lil-309519
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 percent of activity is retained at 80ºC for 20 min). N-Acylation increased its ordered structure by 4 percent and decreased its ß-T1 structure by 2 percent. 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
Texto completo:
DisponíveL
Índice:
LILACS (Américas)
Assunto principal:
Proteínas de Bactérias
/
Proteínas de Choque Térmico
/
Mycobacterium leprae
Tipo de estudo:
Estudo prognóstico
Idioma:
Inglês
Revista:
Braz. j. med. biol. res
Assunto da revista:
Biologia
/
Medicina
Ano de publicação:
2002
Tipo de documento:
Artigo
/
Documento de projeto
País de afiliação:
Brasil
Instituição/País de afiliação:
Instituto Butantan/BR
/
Universidade de Säo Paulo/BR
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