The use of protein structure/activity relationships in the rational design of stable particulate delivery systems

Brazilian Journal of Medical and Biological Research

M.h.b. Costa²  W. Quintilio²  O.a. Sant'anna¹  A. Faljoni-alário¹  P.s. De Araujo¹ 

[1] ,Instituto Butantan Centro de Biotecnologia Laboratório de Microesferas e Lipossomos

关键词: Protein stability;    Hydrophobic modification;    Vaccine delivery system;    Drug delivery system;    Adjuvant;   

DOI  :  10.1590/S0100-879X2002000600014

来源: SciELO

【 摘 要 】

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.

【 授权许可】

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