Sequence diversity of the peptaibol antibiotic suzukacillin-A from the mold Trichoderma viride

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Abstract

From the culture broth of the mold Trichoderma viride, strain 63 C-I, the polypeptide antibiotic suzukacillin (SZ) was isolated. A peptide mixture named SZ-A was obtained by crystallization from crude SZ. Individual peptides from SZ-A were isolated by semipreparative HPLC and sequences were determined by HPLC-ESI-MS. The data confirm a general sequence of SZ-A published previously and in addition establish the individual sequences of 15 acetylated eicosa peptides with C-terminal alcohols. The major peptide SZ-A4 (21% of all peptides) shows the sequence: Ac-Aib-Ala-Aib-Ala-Aib-Ala6-Gln- Aib-Lx9-Aib-Gly-Aib12-Aib -Pro-Vx15-Aib-Vx17-Gln-Gln-Fol. Amino acid exchanges of the peptaibol are located in position 6 (Ala/Aib), 9 (Vx/Lx), 12 (Aib/Lx), 17 (Aib/Vx) and possibly at position15 (Val/Iva) (uncommon abbreviations: Aib (α-aminoisobutyric acid); Iva (D-isovaline); Lx (L-leucine or L-isoleucine); Vx (L-valine or D-isovaline); Fol (L-phenylalaninol)). Copyright © 2005 European Peptide Society and John Wiley & Sons, Ltd.

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Krause, C., Kirschbaum, J., Jung, G., & Brückner, H. (2006). Sequence diversity of the peptaibol antibiotic suzukacillin-A from the mold Trichoderma viride. Journal of Peptide Science, 12(5), 321–327. https://doi.org/10.1002/psc.728

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