79118-33-5Relevant academic research and scientific papers
Cyclopentapeptides as flexible conformational templates
Nikiforovich, Gregory V.,Kbver, Katalin E.,Zhang, Wei-Jun,Marshall, Garland R.
, p. 3262 - 3273 (2000)
Studies of 3D models for cyclopentapeptides (CPP's) employing only NMR spectroscopy encounter a serious problem. Because of conformer averaging, 3D structure(s) derived directly from NMR data may not correspond to the energy minimum (minima) with low rela
Solution synthesis, conformational analysis, and antimicrobial activity of three alamethicin F50/5 analogs bearing a trifluoroacetyl label
De Zotti, Marta,Ballano, Gema,Jost, Micha,Salnikov, Evgeniy S.,Bechinger, Burkhard,Oancea, Simona,Crisma, Marco,Toniolo, Claudio,Formaggio, Fernando
, p. 1163 - 1191 (2014/11/07)
We prepared, by solution-phase methods, and fully characterized three analogs of the membrane-active peptaibiotic alamethicin F50/5, bearing a single trifluoroacetyl (Tfa) label at the N-terminus, at position 9 (central region) or at position 19 (C-termin
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.
The effect of a peptide helix macrodipole on the pKa of an asp side chain carboxylate
Joshi, Hemant V.,Meier, Mark S.
, p. 12038 - 12044 (2007/10/03)
A study of the effect of a helix dipole on the pKa of a side chain functional group has been undertaken to determine the magnitude of these electrostatic effects in the absence of interfering influences from a protein matrix. Three helical pept
