The use of protein structure/activity relationships in the rational design of stable particulate delivery systems.
Braz J Med Biol Res
; 35(6): 727-30, 2002 Jun.
Article
em En
| MEDLINE
| ID: mdl-12045839
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 80 degrees C for 20 min). N-Acylation increased its ordered structure by 4% and decreased its beta-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.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Proteínas de Choque Térmico
/
Mycobacterium leprae
Tipo de estudo:
Prognostic_studies
Idioma:
En
Ano de publicação:
2002
Tipo de documento:
Article