Trichotoxin A40. Purification by counter-current distribution and sequencing of isolated fragments

Brückner, Hans; König, Wilfried Α.; Aydin, Mitat; Jung, Günther

doi:10.1016/0167-4838(85)90100-1

Cited by 44 publications

(17 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…They differ by AA exchange mainly in positions 4 and 11. As a result of related structures the antibiotic and hemolytic properties of TV II are similar to 18-mer peptaibols trichotoxins containing Valol [2][3][4] and hypomurocins B [24]. The latter is a mixture of peptides containing either C-terminal Leuol or Valol.…”

Section: Resultsmentioning

confidence: 93%

“…The structures of seven major 14-mer peptides of the microheterogeneous mixture, comprising at least 21 peptides, could be determined [14,18,19]. The originally proposed name trichotoxin B [1] was changed by us to trichovirins I since the sequences of these 14-mer peptides were different from those of the 18-mer trichotoxins A-40 and A-50 [3,4] isolated from T. viride strain NRRL 5242.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Structures of trichovirins II, peptaibol antibiotics from the moldTrichoderma viride NRRL 5243

1999

Self Cite

View full text Add to dashboard Cite

From the culture broth of the mold Trichoderma viride NRRL 5243 a mixture of polypeptides, named trichovirins (TV), could be isolated and purified by chromatography on XAD-2 adsorber resin and Sephadex LH-20 gel. Chromatography on silica gel using chloroform/methanol 8:2 as eluent provided a mixture of peptides named TV I. Subsequent elution with chloroform/methanol 1:1 yielded a second group of peptides named TV II. That group could be separated into individual components by repetitive HPLC on an octadecylsilyl and a fluorocarbon stationary phase. The sequences of 12 peptides of TV II could be determined by electrospray ionization tandem mass spectrometry of isolated peptides and gas chromatography-mass spectrometry of methanolysates. The N-termini of the 18-mer peptides are acetylated and the C-termini consist of leucinol. Owing to the presence of alpha-aminoisobutyric acid (Aib) residues and the bactericidal and hemolytic activity, the peptides belong to the family of peptaibol antibiotics.

show abstract

Section: Resultsmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Structures of trichovirins II, peptaibol antibiotics from the moldTrichoderma viride NRRL 5243

1999

Self Cite

View full text Add to dashboard Cite

show abstract

“…Subsequently, analytical and preparative trifluoroacetolysis of the peptaibols trichotoxin and suzukacillin was intensively used by Jung and co-workers [15] [16]. It was shown that release of C-terminal peptides occurs, besides the fast scission of the Aib -Pro bond that is followed by cleavages of certain Aib -Aaa bonds (Aaa: Gly, Ala).…”

mentioning

confidence: 99%

Studies on the Selective Trifluoroacetolytic Scission of Native Peptaibols and Model Peptides Using HPLC and ESI‐CID‐MS

Theis

Degenkolb

Brückner

2008

Chemistry & Biodiversity

Self Cite

View full text Add to dashboard Cite

Representative members of a group of linear, N-acylated polypeptide antibiotics (peptaibols) containing alpha-aminoisobutyric acid (Aib) and, in part, isovaline (Iva), as well as proteinogenic amino acids and a C-terminal-bonded 2-amino alcohol, were treated with anhydrous trifluoroacetic acid (TFA) at 37 degrees for 0.5-26 h. The resulting fragments were separated by HPLC and characterized by electrospray ionization collision-induced dissociation mass spectrometry (ESI-CID-MS). The following 16-20-residue peptaibols were investigated: natural, microheterogeneous mixtures of antiamoebins and alamethicin F50, uniform paracelsin A, and synthetic trichotoxin A50/E. In the natural peptides, bonds formed between Aib (Iva) and Pro (Hyp) were rapidly and selectively cleaved within 0.5 h. Furthermore, TFA esters of the C-terminal amino alcohols were formed. Depending on time, release of C-terminal tri- and tetrapeptides as well as amino acids from the major fragments was observed. Synthetic homooligopeptides, namely Z- and Ac-(Aib)(10)-O(t)Bu and Z-(Aib)(7)-O(t)Bu, were analyzed for comparison. On treatment with TFA, a regular series of Z-(Aib)(10-5)-OH from Z-(Aib)(10)-O(t)Bu were detected within 0.5 h, and, after 3 h, release of a regular series of Z-(Aib)(7-3)-OH from Z-(Aib)(7)-O(t)Bu were observed. Moreover, concomitant release of the series of H-(Aib)(10-3)-OH from the decapeptide occurred. From these data, a repetitive cleavage mechanism via intermediate formation of C-terminal oxazolones on trifluoroacetolysis is proposed. Furthermore, their formation and stability in native peptaibols are correlated with subtle structural differences in protein amino acids linked to Aib. From the conspicuous concordance of the formation and abundance of regular series of trifluoroacetolytic fragments and of positive ions of the b-series in CID-MS, the generation of intermediate oxazolonium ions in both gas and liquid phase is concluded.

show abstract

“…We also found 21 yet undescribed trichotoxin sequences obtained as microheterogeneous mixtures produced by members of the Viride clade. Besides T. viride [4,5,14], the production of trichotoxins was also reported in the literature for T. asperellum (clade Hamatum [3,8]) and T. harzianum (clade Harzianum [41]), suggesting that this group of peptaibols can be produced by various subtaxa within the genus Trichoderma. Our results are in agreement with these previous data by confirming the trichotoxin production ability of further T. asperellum and T. viride isolates, and in addition they reveal the production of trichotoxins also in the case of T. viridescens from clade Viride.…”

Section: Discussionmentioning

confidence: 99%

Peptaibol profiles of Iranian Trichoderma isolates

Tamandegani

Zafari

Marik

et al. 2016

Acta Biologica Hungarica

View full text Add to dashboard Cite

Five Iranian Trichoderma isolates from species T. viride, T. viridescens, T. asperellum, T. longibrachiatumand T. citrinoviride -selected from the Fungal Collection of the Bu Ali Sina University, Hamedan, Iran -were investigated for their peptaibol production. All examined isolates showed remarkable antibacterial activities during the screening of their extracts for peptaibol content with a Micrococcus luteus test culture. HPLC-ESI-IT MS was used for identification and elucidation of the amino acid sequences of peptaibols. The detected peptaibol compounds contain 20 or 18 amino acid residues and belong to the trichobrachin and trichotoxin groups of peptaibols, respectively. T. longibrachiatum and T. citrinoviride produced trichobrachins, while trichotoxins could be detected in T. viride, T. viridescens and T. asperellum. Out of 37 sequences detetermined, 26 proved to be new, yet undescribed compounds, while others were identified as previously reported trichotoxins (trichotoxin A-50s and T5D2) and trichobrachins (longibrachins AI, AII, AIII, BII and BIII). Compounds within the two groups of detected peptaibols differed from each other only by a single or just a few amino acid changes.

show abstract

Trichotoxin A40. Purification by counter-current distribution and sequencing of isolated fragments

Cited by 44 publications

References 35 publications

Structures of trichovirins II, peptaibol antibiotics from the moldTrichoderma viride NRRL 5243

Structures of trichovirins II, peptaibol antibiotics from the moldTrichoderma viride NRRL 5243

Studies on the Selective Trifluoroacetolytic Scission of Native Peptaibols and Model Peptides Using HPLC and ESI‐CID‐MS

Peptaibol profiles of Iranian Trichoderma isolates

Contact Info

Product

Resources

About