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Eur J Pharm Sci. 2014 Dec 18;65:112-21. doi: 10.1016/j.ejps.2014.09.012. Epub 2014 Sep 21.

Melittin-glutathione S-transferase fusion protein exhibits anti-inflammatory properties and minimal toxicity.

Author information

1
Department of Biopharmaceutical Sciences, University of Illinois, Chicago, IL 60612-7231, USA.
2
Department of Biopharmaceutical Sciences, University of Illinois, Chicago, IL 60612-7231, USA; Department of Bioengineering, University of Illinois, Chicago, IL 60607-7052, USA; Department of Ophthalmology and Visual Sciences, University of Illinois, Chicago, IL 60612-4319, USA. Electronic address: rag@uic.edu.

Abstract

Although potent, proteins often require chemical modification for therapeutic use. Immunogenicity, difficult synthesis, and scale-up of these modifications are all engineering obstacles that stand in the way of expanding the use of these therapeutics. Melittin, a peptide derived from bee venom, has been shown to modulate inflammation. Although potentially therapeutic, the native peptide causes cell lysis and toxicity significantly hindering therapeutic application. Based upon the knowledge of the pore formation mechanism, we examined the toxicity and therapeutic effect of a melittin fusion protein with glutathione-S-transferase. The fusion of melittin and glutathione S-transferase results in diminished toxicity of the peptide and retained anti-inflammatory properties at doses that exceed toxic concentration of native melittin. Our results suggest that fusion proteins, particularly those of glutathione-S-transferase, may be facile modifications to control protein activity.

KEYWORDS:

Fusion protein; Glutathione S-transferase; Inflammation; Macrophage; Melittin; Protein therapeutic

PMID:
25240321
PMCID:
PMC4253680
DOI:
10.1016/j.ejps.2014.09.012
[Indexed for MEDLINE]
Free PMC Article

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