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The use of protein structure/activity relationships in the rational design of stable particulate delivery systems BJMBR
Costa,M.H.B.; Quintilio,W.; Sant'Anna,O.A.; Faljoni-Alário,A.; Araujo,P.S. de.
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...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Protein stability; Hydrophobic modification; Vaccine delivery system; Drug delivery system; Adjuvant.
Ano: 2002 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2002000600014
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