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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Synthetic and structural studies on Pyrularia pubera thionin: a single-residue mutation enhances activity against Gram-negative bacteria.

The thionin from Pyrularia pubera (Pp-TH), a 47-residue peptide with four internal disulfide bonds, was efficiently produced by chemical synthesis. Its antimicrobial activity in vitro against several representative pathogens (EC(50)=0.3-3.0 microM) was identical to that of natural Pp-TH. This peptide has a unique Asp(32) instead of the consensus Arg found in other thionins of the same family. In order to evaluate the effect of this mutation, the Arg(32) analogue (Pp-TH(D32R)) was also synthesized and showed a significant increase in antibiotic activity against several Gram-negative bacteria, whereas it retained the same activity against other pathogens. The overall structure of Pp-TH(D32R) was maintained, though a slight decrease in the helical content of the peptide was observed.[1]

References

  1. Synthetic and structural studies on Pyrularia pubera thionin: a single-residue mutation enhances activity against Gram-negative bacteria. Vila-Perelló, M., Sánchez-Vallet, A., García-Olmedo, F., Molina, A., Andreu, D. FEBS Lett. (2003) [Pubmed]
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