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A new family of N-terminally truncated peptaibols from the biocontrol fungus trichoderma harzianum

 
: Degenkolb, T.; Röhrich, C.R.; Vilcinscas, A.; Döhren, H. von; Brückner, H.

Journal of peptide science 22 (2016), Supplement S2, pp.S98
ISSN: 1075-2617
ISSN: 1099-1387
European Peptide Symposium (EPS) <34, 2016, Leipzig>
International Peptide Symposium (IPS) <8, 2016, Leipzig>
English
Abstract
Fraunhofer IME ()

Abstract
Peptaibiotics and their subgroup of peptaibols are defined as bioactive microbial peptides containing the characteristic, non-proteinogenic α-aminoisobutyric acid (Aib). They are of permanent interest to both academics and industry owing to their manifold biological activities including unique membrane-modifying properties. Here we report on the sequences of a new class of truncated 16-residue peptaibol-derived peptides isolated from agar plate cultures of the filamentous fungus T. harzianum CBS 226.95. These peptides are the result of an unexpected endoenzymatic cleavage of the N-terminal dipeptide AcAib1-Ser2 from concomitantly produced 18-residue peptaibols, which are structurally related to trichokindins. They display the general sequence AcAib1-Ser2-↓Ala3-(Aaa)4-17-Xol18 (Aaa, amino acid including Aib; Xol, Leuol/Ileol). The biosynthesis of twelve 18-residue trichokindin-type peptaibols and of six truncated 16-residue peptaibiotics with free N-alanyl termini derived thereof (cleavage indicated by arrow), named brevikindins I - VI, provides new insights into the mechanism of non-ribosomal peptaibotic biosynthesis and plant-protective properties of T. harzianum.

: http://publica.fraunhofer.de/documents/N-467437.html