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Sequence diversity of the peptaibol antibiotic suzukacillin‐A from the mold Trichoderma viride
Author(s) -
Krause Corina,
Kirschbaum Jochen,
Jung Günther,
Brückner Hans
Publication year - 2006
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.728
Subject(s) - peptide , valine , amino acid , chemistry , leucine , peptide sequence , sequence (biology) , pentapeptide repeat , isoleucine , stereochemistry , biochemistry , gene
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‐Ala 6 ‐Gln‐Aib‐Lx 9 ‐Aib‐Gly‐Aib 12 ‐Aib‐Pro‐Vx 15 ‐Aib‐Vx 17 ‐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.