Minor sequence variants are underlined in the sequences. This JAK activation applies to all sequence https://www.selleckchem.com/products/Trichostatin-A.html tables Screening of Hypocrea gelatinosa. A single strain
(ICMP 5417) of this species has previously been screened positive Aib and Iva by a GC/MS-based approach (Brückner et al. 1991). From the specimen of H. gelatinosa, 14 compounds 14−27, six 18-residue and eight 19-residue peptaibols, were sequenced. All of them but compounds 14 and 18 are new (Tables 6 and 7, Table S2a and S2b; Fig. 2a). The 18-residue sequences, compounds 19−21, 23, 25, and 27, named gelatinosins B 1−6, resemble hypomurocins6 or neoatroviridins7. Two of the 19-residue sequences, compounds 14 and 18, are identical with the recently described hypopulvins from H. pulvinata (Röhrich et al. 2012). The selleck products new compounds 15−17, 22, and 24, named gelatinosins A 1−5, exhibit a partially new building scheme − the residue in position 5 of the peptide chain was assigned as Phe, based upon HR-MS/MS data. In contrast to this, the new 19-residue compound 26 displays a different building scheme, resembling trichostrigocinsA/B (Degenkolb et al. 2006a). The plate culture of H. gelatinosa was shown to produce three minor 11-residue SF4-peptaibols, compounds 6, 29, and 33, and nine gelatinosins B (compounds, 19, 20, 25, 27, 28, 30−32, and 34), 18-residue peptaibols of the hypomurocin/neoatroviridin-type.
However, 19-residue peptaibols have not been detected (Tables 6 and 7, Table S2a and S2b; Fig. 2b). tR [min] [M + H]+ Residuea 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 14 37.1–37.3 1866.0929 Ac Aib Ala Ala Ala Aib Gln Aib Lxx Aib Gly Lxx Aib Pro Vxx Aib Aib Gln Gln Pheol 15 37.7–37.8 GBA3 1895.1067 Ac Aib Ala Aib Aib Phe Gln
Aib Aib Aib Gly Lxx Aib Pro Vxx Aib Aib Glu Gln Lxxol 16 38.0–38.2 1908.1358 Ac Aib Ala Aib Aib Phe Gln Aib Aib Aib Gly Lxx Aib Pro Lxx Aib Aib Gln Gln Lxxol 17 38.8–38.9 1909.1186 Ac Aib Ala Aib Aib Phe Gln Aib Aib Aib Gly Lxx Aib Pro Lxx Aib Aib Glu Gln Lxxol 18 39.5–39.6 1880.1083 Ac Aib Ala Ala Ala Aib Gln Aib Lxx Aib Ala Lxx Aib Pro Vxx Aib Aib Gln Gln Pheol 19 40.2–40.4 1762.0856 Ac Aib Ser Ala Lxx Aib Gln Aib Lxx Aib Gly Vxx Aib Pro Lxx Aib Aib Gln – Lxxol 20 40.9–41.1 1762.0840 Ac Aib Ser Ala Lxx Aib Gln Vxx Lxx Aib Gly Vxx Aib Pro Lxx Aib Aib Gln – Vxxol 21 41.2–41.4 1776.1023 Ac Aib Ser Ala Lxx Vxx Gln Aib Lxx Aib Gly Vxx Aib Pro Lxx Aib Aib Gln – Lxxol 22 41.9 1952.1674 Ac Aib Ala Aib Aib Phe Gln Aib Aib Aib Ser Lxx Aib Pro Lxx Vxx Aib Gln Gln Lxxol 23 42.1–42.3 1776.1023 Ac Aib Ser Ala Lxx Vxx Gln Vxx Lxx Aib Gly Vxx Aib Pro Lxx Aib Aib Gln – Vxxol 6 42.3 1203.8117 Ac Vxx Gln Lxx Lxx Aib Pro Lxx Lxx Aib Pro Lxxol 24 42.9 1953.