79118-36-8Relevant 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.
Crystallographic characterization of helical secondary structures in 2:1and 1:2 α/Β-peptides
Choi, Soo Hyuk,Guzei, Ilia A.,Spencer, Lara C.,Gellman, Samuel H.
experimental part, p. 2917 - 2924 (2009/07/30)
Oligomers containing both α- and β-amino acid residues ("α/β-peptides") are intriguing as potential foldamers. A large setof α/β-peptide backbones can be generated by combining &alph a; and β-amino acid residues in different patterns; however, most resear
Emerimicins III and IV and their ethylalanine12 epimers. Facilitated chemical-enzymatic synthesis and a qualitative evaluation of their solution structures
Slomczynska, Urszula,Beusen, Denise D.,Zabrocki, Janusz,Kociolek, Karol,Redlinski, Adam,Rensser, Fritz,Hutton, William C.,Leplawy, Miroslaw T.,Marshall, Garland R.
, p. 4095 - 4106 (2007/10/02)
The peptaibol antibiotics, emerimicin III and IV (Ac-Phe1-MeA2-MeA3-MeA4-VaI 5-Gly6-Leu7-MeA8-MeA 9-Hyp10-Gln11-R-EtA12-Hyp
PyBOP and PyBroP: Two reagents for the difficult coupling of the α,α-dialkyl amino acid, Aib
Frerot, Eric,Coste, Jacques,Pantaloni, Antoine,Dufour, Marie-Noelle,Jouin, Patrick
, p. 259 - 270 (2007/10/02)
The difficult coupling of α-aminoisobutyric acid (Aib) was carried out using PyBOP and PyBroP in a comparative study with BOP and BroP. These reagents gave good results under simple conditions (one pot, r.t., 1h). Coded amino acids could be coupled with Aib using PyBOP under standard conditions of peptide synthesis without racemization whereas the coupling of two Aib residues required PyBroP/DMAP. A fragment containing an Aib C-terminal could be coupled without epimerization of the penultimate residue.
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
