| Registro completo |
| Provedor de dados: |
BJMBR
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| País: |
Brazil
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| Título: |
The use of protein structure/activity relationships in the rational design of stable particulate delivery systems
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| Autores: |
Costa,M.H.B.
Quintilio,W.
Sant'Anna,O.A.
Faljoni-Alário,A.
Araujo,P.S. de
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| Data: |
2002-06-01
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| Ano: |
2002
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| Palavras-chave: |
Protein stability
Hydrophobic modification
Vaccine delivery system
Drug delivery system
Adjuvant
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| 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.
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| Tipo: |
Info:eu-repo/semantics/other
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| Idioma: |
Inglês
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| Identificador: |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2002000600014
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| Editor: |
Associação Brasileira de Divulgação Científica
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| Relação: |
10.1590/S0100-879X2002000600014
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| Formato: |
text/html
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| Fonte: |
Brazilian Journal of Medical and Biological Research v.35 n.6 2002
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| Direitos: |
info:eu-repo/semantics/openAccess
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