The conformational preferences of the alicyclic C","-disubstituted glycines Ac,c (I-amino-I-cycloalkane-carboxylic acid; n = 4 , 7, 9, 1 2 ) were assessed in selected model compounds, including homopeptides and Ala (or Aib, a-aminoisobutyric acid)lAc,c peptides containing a small total number of res
Preferred conformation of peptides from Cα,α-symmetrically disubstituted glycines: Aromatic residues
✍ Scribed by M. Crisma; G. Valle; G. M. Bonora; C. Toniolo; F. Lelj; V. Barone; F. Fraternall; P. M. Hardy; H. L. S. Maia
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1991
- Tongue
- English
- Weight
- 249 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
The conformational preference of C^α,α^‐diphenylglycinc (Døg) and C^α,α^‐dibenzylglycine (Dbz) residues was assessed in selected derivatives and small peptides by conformational energy computations, ir absorption, ^1^H‐nmr, and x‐ray diffraction. Conformational energy computations on the two monopeptides strongly support the view that these C^α,α^‐symmetrically disubstituted glycines are conformationally restricted and that their minimum energy conformation falls in the fully extended (C~5~) region. The results of the theoretical analyses appear to be in agreement with the solution and crystal‐state structural propensities of three derivatives and seven di‐and tripeptides.
📜 SIMILAR VOLUMES
A series of N-and C-protected, monodispersed homo-oligopeptides (to the pentamer level) from the cycloaliphatic C Y -dialkylated glycine 1-aminocyclononane-1-carboxylic acid (Ac W c) and two Ala/Ac W c tripeptides have been synthesized by solution methods and fully characterized. The conformational
Recent studies on the conformational preferences of the Dg (C ␣,␣ -diphenylglycine) residue showed that this C ␣,␣ -disubstituted glycine has a structural versatility. In fact, depending on the nature of the following or preceding residue, Dg can assume either folded or extended conformations. We ha
The lipophilic, chiral, C h -methylated h-amino acid L-(h Me)Aoc (2-methyl-2-amino-octanoic acid) was prepared using a chemo-enzymatic approach. Two series of terminally protected model peptides, from dimer through to hexamer, containing L-(h Me)Aoc in combination with either Gly or Aib, were synthe
The crystal-state molecular structures of five linear A0,c homo-oligopeptides to the tetramer were determined by x-ray diffraction. The oligomem are H-(Aw),-OMe, Fmoc-(Ac+),-OMe . MeOH, Ac-(Ac&,-OMe, pBrBz-(Aq&OMe. H20, and t-Boc-(Ac+),-OMe . 2Hz0. The results indicate the propensity of the tri-and