FEBS Letters | |
Synthetic and structural studies on Pyrularia pubera thionin: a single‐residue mutation enhances activity against Gram‐negative bacteria | |
Sánchez-Vallet, Andrea1  Andreu, David2  Vila-Perelló, Miquel2  Garcı́a-Olmedo, Francisco1  Molina, Antonio1  | |
[1] Laboratory of Biochemistry, Department of Biotechnology, UPM-ETSIA, Avda. Complutense, E-28040 Madrid, Spain;Department of Experimental and Health Sciences, Pompeu Fabra University, Dr. Aiguader 80, E-08003 Barcelona, Spain | |
关键词: Thionin; Antimicrobial peptide; Oxidative folding; Plant; Boc; tert-butyloxycarbonyl; tBu; tert-butyl; Trt; trityl; Fmoc; 9-fluorenylmethoxycarbonyl; DMF; dimethylformamide; HPLC; high performance liquid chromatography; MALDI-TOF MS; matrix-assisted laser desorption ionization time of flight mass spectrometry; TFA; trifluoroacetic acid; GSH; reduced glutathione; GSSG; oxidized glutathione; CD; circular dichroism; | |
DOI : 10.1016/S0014-5793(03)00053-X | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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 (EC50=0.3–3.0 μM) was identical to that of natural Pp-TH. This peptide has a unique Asp32 instead of the consensus Arg found in other thionins of the same family. In order to evaluate the effect of this mutation, the Arg32 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.
【 授权许可】
Unknown
【 预 览 】
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