The use of protein structure/activity relationships in the rational design of stable particulate delivery systems
| Autor: | M.H.B. Costa, W. Quintilio, O.A. Sant'Anna, A. Faljoni-Alário, P.S. de Araujo |
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| Jazyk: | angličtina |
| Rok vydání: | 2002 |
| Předmět: | |
| Zdroj: | Brazilian Journal of Medical and Biological Research, Vol 35, Iss 6, Pp 727-730 (2002) |
| Druh dokumentu: | article |
| ISSN: | 0100-879X 1414-431X |
| DOI: | 10.1590/S0100-879X2002000600014 |
| Popis: | 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. |
| Databáze: | Directory of Open Access Journals |
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