Conformational studies on host-guest peptides containing chiral α-methyl-α-amino acids
✍ Scribed by ALTMANN, EVA ;ALTMANN, KARL-HEINZ ;NEBEL, KURT ;MUTTER, MANFRED
- Book ID
- 115098827
- Publisher
- Wiley (Blackwell Publishing)
- Year
- 2009
- Tongue
- English
- Weight
- 514 KB
- Volume
- 32
- Category
- Article
- ISSN
- 0367-8377
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The conformational preferences of linear peptides containing a,a-disubstituted a-amino acids, derived from the crystal structures of 28 compounds, are reviewed. In particular, the sensitivity of peptide conformation to the geometry of these unusual amino acids is underlined. We also consider possibl
## Abstract For Abstract see ChemInform Abstract in Full Text.
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
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## Abstract A single chiral cyclic α,α‐disubstituted amino acid, (3__S__,4__S__)‐1‐amino‐(3,4‐dimethoxy)cyclopentanecarboxylic acid [(__S__,__S__)‐Ac~5~c^dOM^], was placed at the __N__‐terminal or __C__‐terminal positions of achiral α‐aminoisobutyric acid (Aib) peptide segments. The IR and ^1^H NMR