The use of protein structure/activity relationships in the rational design of stable particulate delivery systems
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...
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Associação Brasileira de Divulgação Científica
2002-06-01
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doaj-35841e6d9ad7459fa2190fc50a2ced7c2020-11-24T22:39:58ZengAssociação Brasileira de Divulgação CientíficaBrazilian Journal of Medical and Biological Research0100-879X1414-431X2002-06-0135672773010.1590/S0100-879X2002000600014The use of protein structure/activity relationships in the rational design of stable particulate delivery systemsM.H.B. CostaW. QuintilioO.A. Sant'AnnaA. Faljoni-AlárioP.S. de AraujoThe 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.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2002000600014Protein stabilityHydrophobic modificationVaccine delivery systemDrug delivery systemAdjuvant |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
M.H.B. Costa W. Quintilio O.A. Sant'Anna A. Faljoni-Alário P.S. de Araujo |
spellingShingle |
M.H.B. Costa W. Quintilio O.A. Sant'Anna A. Faljoni-Alário P.S. de Araujo The use of protein structure/activity relationships in the rational design of stable particulate delivery systems Brazilian Journal of Medical and Biological Research Protein stability Hydrophobic modification Vaccine delivery system Drug delivery system Adjuvant |
author_facet |
M.H.B. Costa W. Quintilio O.A. Sant'Anna A. Faljoni-Alário P.S. de Araujo |
author_sort |
M.H.B. Costa |
title |
The use of protein structure/activity relationships in the rational design of stable particulate delivery systems |
title_short |
The use of protein structure/activity relationships in the rational design of stable particulate delivery systems |
title_full |
The use of protein structure/activity relationships in the rational design of stable particulate delivery systems |
title_fullStr |
The use of protein structure/activity relationships in the rational design of stable particulate delivery systems |
title_full_unstemmed |
The use of protein structure/activity relationships in the rational design of stable particulate delivery systems |
title_sort |
use of protein structure/activity relationships in the rational design of stable particulate delivery systems |
publisher |
Associação Brasileira de Divulgação Científica |
series |
Brazilian Journal of Medical and Biological Research |
issn |
0100-879X 1414-431X |
publishDate |
2002-06-01 |
description |
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. |
topic |
Protein stability Hydrophobic modification Vaccine delivery system Drug delivery system Adjuvant |
url |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2002000600014 |
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