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Structure of a new cyclotetrapeptide trapoxin A
H Nakai1, K Nagashima, H Itazaki
1Shionogi Research Laboratories, Shionogi & Co. Ltd, Osaka, Japan.
Summary
The crystal structure of trapoxin A was determined, revealing cyclo[-(S)-phenylalanyl-(S)-phenylalanyl-(R)-pipecolinyl-(2S,9S)-2-amino-8-oxo-9,10-epoxydecanoyl-]. Three independent molecules form infinite chains via hydrogen bonds.
Area of Science:
- Chemical Crystallography
- Structural Biology
- Organic Chemistry
Background:
- Trapoxin A is a cyclic peptide with potential biological activity.
- Understanding its precise three-dimensional structure is crucial for structure-activity relationship studies.
Purpose of the Study:
- To elucidate the detailed crystal structure of trapoxin A.
- To provide a precise molecular model for future drug design and mechanistic studies.
Main Methods:
- Single-crystal X-ray diffraction was employed to determine the structure.
- The crystal structure was solved and refined using standard crystallographic techniques.
Main Results:
- The molecular formula was determined as C34H42N4O6 with a molecular weight of 602.73.
- The crystal system is triclinic, space group P1, with three crystallographically independent molecules in the unit cell.
- The structure revealed a specific cyclic arrangement of amino acid residues and an epoxide moiety, with intermolecular NH...O hydrogen bonds forming infinite chains.
Conclusions:
- The precise crystal structure of trapoxin A has been determined.
- The observed hydrogen bonding network provides insights into crystal packing and intermolecular interactions.