What question did this study set out to answer?

This research aims to explore the structural changes in the ribavirin polymorphs under high pressure.

May 16, 2026Open Access

Compression of Ribavirin to 35 GPa

BTBhaskar TiwariDeutsches Elektronen-Synchrotron DESY SPSimon ParsonsJoint Laboratory for Extreme Conditions Matter Properties NGNico GiordanoDeutsches Elektronen-Synchrotron DESY

Key Points

This research aims to explore the structural changes in the ribavirin polymorphs under high pressure.
Ribavirin forms were recrystallized at high-pressure and high-temperature using a diamond anvil cell.
Single crystals were subjected to compression up to 35.1 GPa and analyzed through X-ray diffraction.
Structural responses were observed at varying pressures, specifically near 10.9 and 26.6 GPa.
The orthorhombic phase (P212121) of ribavirin is maintained under compression.
Structural responses include changes in c-axis compressibility and ribofuranosyl ring conformation.
The hydrogen-bond topology remains unchanged even at the highest pressures.

Abstract

The antiviral pharmaceutical compound ribavirin has two known crystalline polymorphs, V1 and V2, under ambient conditions. The V2 form is thermodynamically favored and more readily obtained. The higher-density V1 form was obtained by high-pressure, high-temperature recrystallization in a diamond anvil cell. Recovered single crystals were compressed to 35.1 GPa and characterized by X-ray diffraction. The orthorhombic phase (P212121) is retained throughout compression, with changes in structural response near 10.9 and 26.6 GPa reflected by variations in c-axis compressibility and ribofuranosyl ring conformation. Compression proceeds from interlayer void collapse to progressive layer flattening and ultimately to intramolecular conformational adjustment once residual free volume is exhausted. The principal hydrogen-bond topology is preserved to the highest pressures investigated.

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