Materials 2009, 2(3), 765-775; doi:10.3390/ma2030765
Article

Hoffmeister Series Ions Protect Diphtheria Toxoid from Structural Damages at Solvent/Water Interface

1 Laboratório de Microesferas e Lipossomas – Centro de Biotecnologia- I. Butantan, Av. Vital Brasil, 1500, 05503-900 - Butantan, São Paulo, SP, Brasil 2 Divisão de Desenvolvimento Tecnológico e Produção-I. Butantan Av. Vital Brasil, 1500 (05503-900) Butantan, São Paulo, SP, Brasil 3 I. de Química, (05508-000) Universidade de São Paulo Av. Lineu Prestes 748, São Paulo, SP, Brasil # Present affiliation: Novartis, Brazil
* Author to whom correspondence should be addressed.
Received: 1 June 2009; Accepted: 11 July 2009 / Published: 13 July 2009
(This article belongs to the Special Issue Biocompatibility of Materials)
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Abstract: During the W1/O phase (in the W1/O/W2 process) of protein microencapsulation within poly-lactide-co-glycolide (PLGA), hydrophobic interfaces are expanded where interfacial adsorption occurs followed by protein unfolding and aggregation. Spectroscopic and immunological techniques were used to ascertain the effects of the Hoffmeister series ions on Diphtheria toxoid (Dtxd) stability during the W1/O phase. A correlation was established between salts used in aqueous solutions and the changes in Dtxd solubility and conformation. The Dtxd α-helical content was quite stable thus leading to the conclusion that encapsulation was followed by protein aggregation, with minor exposition of hydrophobic residues and a small change at the S-S dihedral angle. Dtxd aggregation is 95% avoided by the chaotropic SCN-. This was used to prepare a stable Dtxd and immunologically recognized/PLGA formulation in the presence of 30 mM SNC-. The recovery increased by 10.42% or 23.2% when microencapsulation was within the -COOMe or -COOH (12kDa) PLGA, respectively. In conclusion, the aim of this work was achieved, which was to obtain the maximum of Dtxd stability after contact with CH2Cl2 to begin its PLGA microencapsulation within ideal conditions. This was a technological breakthrough because a simple solution like salt addition avoided heterologous proteins usage.
Keywords: Hoffmeister series ions; protein solubilization; protein stabilization; interaction protein/organic solvent; protein microencapsulation; adjuvant particulate; adjuvant

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MDPI and ACS Style

Namur, J.A.; Takata, C.S.; De Araujo, P.S.; Bueno-da-Costa, M.H. Hoffmeister Series Ions Protect Diphtheria Toxoid from Structural Damages at Solvent/Water Interface. Materials 2009, 2, 765-775.

AMA Style

Namur JA, Takata CS, De Araujo PS, Bueno-da-Costa MH. Hoffmeister Series Ions Protect Diphtheria Toxoid from Structural Damages at Solvent/Water Interface. Materials. 2009; 2(3):765-775.

Chicago/Turabian Style

Namur, Jocimara A.; Takata, Célia S.; De Araujo, Pedro S.; Bueno-da-Costa, Maria H. 2009. "Hoffmeister Series Ions Protect Diphtheria Toxoid from Structural Damages at Solvent/Water Interface." Materials 2, no. 3: 765-775.

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