124125-97-9Relevant academic research and scientific papers
Synthesis, preferred conformation, and membrane activity of medium-length peptaibiotics: Tylopeptin B
Gobbo, Marina,Poloni, Claudia,De Zotti, Marta,Peggion, Cristina,Biondi, Barbara,Ballano, Gema,Formaggio, Fernando,Toniolo, Claudio
experimental part, p. 169 - 181 (2011/02/23)
The solid-phase synthesis and full chemical characterization of the medium-length (14-amino acid residues) peptaibol with antibiotic properties of tylopeptin B, originally extracted from the fruiting body of the mushroom Tylopilus neofelleus, are described. These data are accompanied by the results on the solution-phase synthesis via the segment condensation approach of a selected, side-chain protected, analog. A solution conformational analysis, performed by the combined use of FTIR absorption, circular dichroism, and 2D-NMR (the latter technique coupled to molecular dynamics calculations), favors the conclusion that the 3D-structure of tylopeptin B is largely helical with a preference for the α- or the 310-helix type depending upon the nature of the solvent. Helix topology and (partial) amphiphilic character are responsible for the observed membrane-modifying properties of this peptaibiotic.
Rapid and efficient synthesis of peptide fragments containing α- aminoisobutyric acid using Fmoc-amino acid chlorides/potassium salt of 1- hydroxybenzotriazole
Suresh Babu, Vommina V.,Gopi, Hosahudya N.
, p. 1049 - 1050 (2007/10/03)
The synthesis of peptides containing multiple Aib residues was accomplished using Fmoc-Aib-Cl in presence of KOBt. As no additional base was added, the duration of coupling reactions could be extended. Thus, the synthesis of the alamethicin 1-4 fragment, Aib-Pro-Aib-Ala, the emerimicin 2- 6 fragment, Aib-Aib-Aib-Val-Gly and the Aib tetramer, Fmoc-(Aib)4-OBzl were accomplished in good yield and purity.
Determination of an 8-? interatomic distance in a helical peptide by solid-state NMR spectroscopy
Holl, Susan M.,Marshall, Garland R.,Beusen, Denise D.,Kociolek, Karol,Redlinski, Adam S.,Leplawy, Miroslaw T.,McKay, Robert A.,Vega, Shimon,Schaefer, Jacob
, p. 4830 - 4833 (2007/10/02)
The combination of transferred-echo double resonance (TEDOR) with rotational-echo double resonance (REDOR) has been used to measure an 8-? fluorine-carbon internuclear distance in a nine-residue fragment of the peptide antibiotic emerimicin. The fragment is 19FCH2CO-Phe-MeA-MeA-[1-13C]MeA-[ 15N]Val-Gly-Leu-MeA-MeA-OBzl (MeA = α-methylalanine or aminoisobutyric acid). The TEDOR part of this magic-angle-spinning, solid-state NMR experiment selects the 13C label by its dipolar coupling to 15N and suppresses the natural-abundance carbon background. The REDOR part of the experiment measures dipolar coupling of the selected carbon to 19F. The TEDOR-REDOR combined experiment works with a variety of spin 1/2 nuclei and can be used to characterize internuclear distances and geometry in macromolecular aggregates that do not crystallize.
Determination of a precise interatomic distance in a helical peptide by REDOR NMR
Marshall, Garland R.,Beusen, Denise D.,Kociolek, Karol,Redlinski, Adam S.,Leplawy, Miroslaw T.,Pan, Yong,Schaefer, Jacob
, p. 963 - 966 (2007/10/02)
A new spectroscopic technique, rotational-echo double-resonance (REDOR) NMR, for solids utilizes magic-angle spinning and measures directly the dipolar coupling between stable-isotope-labeled nuclei and, thus, interatomic distances. REDOR has been used to
