1. The crystal structures of the synthetic C-terminal octa- and dodecapeptides of trichovirin
R Gessmann, P Benos, H Brückner, M Kokkinidis J Pept Sci. 1999 Feb;5(2):83-95. doi: 10.1002/(SICI)1099-1387(199902)5:23.0.CO;2-U.
The structures of two synthetic peptides with sequences corresponding to the C-terminal region of the naturally occurring 14-residue peptaibol trichovirin have been determined. The crystal structures of 8- and 12-residue segments are presented and are compared with the structures of the tetrapeptide and of the 9-residue segment, which have been reported earlier. A comparison between these segments leads to the hypothesis that the three-dimensional structure of trichovirin is to a large extent determined by the properties of a periodically repeating -Aib-Pro- pattern in the sequence of the peptide.
2. Total synthesis in solution and conformational analysis of the peptaibol cervinin and selected analogues
Chiara Baldini, Massimo Bellanda, Cristina Peggion, Albert Legrand Djontu, Come Atagua, Stefano Mammi, Claudio Toniolo Chem Biodivers. 2007 Jun;4(6):1129-43. doi: 10.1002/cbdv.200790101.
The total synthesis in solution and chemical characterization of the antibacterial undecamer peptaibol cervinin, its C-terminal (Lol-Ac) derivative, also naturally occurring, and three selected analogues modified at the N- and/or C-terminus(i) to improve the affinity to the membrane environment, are described. A solution conformational analysis in different media, performed by the combined use of FT-IR, CD, and 2D-NMR techniques, clearly shows a significant 3(10)-like helicity for these Aib-Pro rich peptides. The hydrophilicity/lipophilicity characteristics of the final compounds significantly influence their membrane-modifying properties.
3. Sequence diversity of the peptaibol antibiotic suzukacillin-A from the mold Trichoderma viride
Corina Krause, Jochen Kirschbaum, Günther Jung, Hans Brückner J Pept Sci. 2006 May;12(5):321-7. doi: 10.1002/psc.728.
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
