The use of protein structure/activity relationships in the rational design of stable particulate delivery systems
Braz. j. med. biol. res
; 35(6): 727-730, June 2002. ilus, tab
Article
in English
| LILACS
| ID: lil-309519
Responsible library:
BR1.1
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 percent of activity is retained at 80ºC for 20 min). N-Acylation increased its ordered structure by 4 percent and decreased its ß-T1 structure by 2 percent. 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
Full text:
Available
Collection:
International databases
Health context:
Neglected Diseases
Health problem:
Leprosy
/
Neglected Diseases
Database:
LILACS
Main subject:
Bacterial Proteins
/
Heat-Shock Proteins
/
Mycobacterium leprae
Type of study:
Prognostic study
Language:
English
Journal:
Braz. j. med. biol. res
Journal subject:
Biology
/
Medicine
Year:
2002
Document type:
Article
/
Project document
Affiliation country:
Brazil
Institution/Affiliation country:
Instituto Butantan/BR
/
Universidade de Säo Paulo/BR