Abstract
The crystal structures of N-alkylated hydrophobic amino acids, including five new compounds, show robust and characteristic hydrogen bond patterns.
Highlights
The crystal structures of hydrophobic amino acids, as chiral substances or racemates, permit systematic investigations of recurring hydrogen bonding patterns due to the absence of side chain functional groups that otherwise could have interfered with the interactions between the charged amino and carboxylate groups
All crystal structures of hydrophobic amino acids reported to date have the same basic layout
A most interesting comparison can be made between the structure of NiPrV and its racemate NiPrVR. Examples exist, such as L-Ala and DL-Ala,[17] it is very uncommon for a racemate to share hydrogen bonding pattern and general packing arrangement with the corresponding enantiomerically pure compound
Summary
The crystal structures of hydrophobic amino acids, as chiral substances or racemates, permit systematic investigations of recurring hydrogen bonding patterns due to the absence of side chain functional groups that otherwise could have interfered with the interactions between the charged amino and carboxylate groups. These were selected to explore the effect of variable side chain bulks, including an interchange of hydrophobic groups between the amino group and the Cα carbon atom [N-isopropyl-Lphenylalanine (NiPrF) and N-benzyl-L-valine (NBnV)], and the effect of going from N-isopropyl-L-valine (NiPrV) to its racemate N-isopropyl-DL-valine (NiPrVR) as well as to the higher analogue N-isopropyl-L-leucine (NiPrL).
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