Research Article
Enhanced activity of an insecticidal protein, trypsin modulating oostatic factor (TMOF), through conjugation with aliphatic polyethylene glycol
Article first published online: 24 JUN 2011
DOI: 10.1002/ps.2219
Copyright © 2011 Society of Chemical Industry
Additional Information
How to Cite
Jeffers, L. A., Shen, H., Khalil, S., Bissinger, B. W., Brandt, A., Gunnoe, T. B. and Roe, R. M. (2012), Enhanced activity of an insecticidal protein, trypsin modulating oostatic factor (TMOF), through conjugation with aliphatic polyethylene glycol. Pest. Manag. Sci., 68: 49–59. doi: 10.1002/ps.2219
Publication History
- Issue published online: 20 DEC 2011
- Article first published online: 24 JUN 2011
- Manuscript Accepted: 2 MAY 2011
- Manuscript Revised: 25 APR 2011
- Manuscript Received: 29 OCT 2010
- Abstract
- Article
- References
- Cited By
Keywords:
- trypsin modulating oostatic factor;
- TMOF;
- PEGylation;
- polyethylene glycol;
- mosquito;
- tobacco budworm;
- cotton bollworm;
- protein delivery
Abstract
BACKGROUND: Trypsin modulating oostatic factor (TMOF), a decapeptide (Tyr-Asp-Pro-Ala-Pro6) isolated from the ovaries of the adult yellow fever mosquito, Aedes aegypti, regulates trypsin biosynthesis. TMOF per os is insecticidal to larval mosquitoes and a good model for the development of technologies to enhance protein insecticide activity by reduced catabolism and/or enhanced delivery to the target.
RESULTS: TFA-TMOF-K (TFA = trifluoro acetyl) allowed the specific conjugation of monodispersed, aliphatic polyethylene glycol (PEG) to the amino group of lysine-producing TMOF-K-methyl(ethyleneglycol)7-O-propionyl (TMOF-K-PEG7P). The addition of lysine to TMOF reduced its per os larval mosquitocidal activity relative to the parent TMOF, but conjugation of TMOF-K with methyl(ethyleneglycol)7-O-propionyl increased its toxicity 5.8- and 10.1-fold above that of TMOF and TMOF-K for Ae. aegypti. Enhanced insecticidal activity was also found for larval Ae. albopictus and for neonates of Heliothis virescens and Heliocoverpa zea. Only TMOF-K was found by MS/MS in the hemolymph for H. virescens fed on TMOF-K-PEG7P. No TMOF, TMOF-K or PEGylated TMOF-K was detected in the hemolymph after topical applications.
CONCLUSIONS: This research suggests that aliphatic PEG polymers can be used as a new method for increasing the activity of insecticidal proteins. Copyright © 2011 Society of Chemical Industry

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