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L-Tryptophan formic acid solvate at 183 K
Christian B Hübschle1, Birger Dittrich, Peter Luger
1Institut für Chemie, Kristallographie, Freie Universität Berlin, Takustrasse 6, 14195 Berlin, Germany.
Acta Crystallographica. Section C, Crystal Structure Communications
|September 3, 2002
Summary
This study reveals that in the crystal structure of L-tryptophan and formic acid at 183 K, L-tryptophan exists as a zwitterion. A strong hydrogen bond forms between neutral formic acid and the tryptophan carboxylate group.
Area of Science:
- Crystallography
- Molecular interactions
- Biochemistry
Background:
- L-tryptophan is an essential amino acid with a crucial role in protein synthesis and neurotransmitter production.
- Understanding the solid-state behavior of amino acids and their interactions with small molecules provides insights into biological processes and drug formulation.
Purpose of the Study:
- To elucidate the crystal structure and intermolecular interactions of the L-tryptophan-formic acid co-crystal at low temperature.
- To characterize the hydrogen bonding network within the compound.
Main Methods:
- Single-crystal X-ray diffraction at 183 K.
- Analysis of crystallographic data to determine molecular conformations and hydrogen bond geometry.
Main Results:
- The crystal structure of C(11)H(12)N(2)O(2).CH(2)O(2) was determined at 183 K.
- L-tryptophan was observed in its zwitterionic form.
- Formic acid was present as a neutral molecule.
- A strong intermolecular hydrogen bond (O-H---O) was identified between the formic acid and the L-tryptophan carboxylate group, with a short O---O distance of 2.487 Å.
Conclusions:
- The study confirms the zwitterionic nature of L-tryptophan in the presence of formic acid under specific conditions.
- The strong hydrogen bond highlights the potential for co-crystallization to modify the properties of L-tryptophan.