Stoichiometric Binding of Cyclophilin‐A to The HIV‐1 Capsid Modulates Its Mechanoelastic Properties (Small 61/2026)

Nanomechanics The HIV-1 capsid is a protein nanocapsule that must remain stable enough to protect the viral genome while deformable enough to traverse the nuclear pore. In Research Article e75453, Juan R. Perilla and co-workers utilize atomic force microscopy simulations to elucidate how Cyclophilin A binding modulates capsid brittleness, revealing a stoichiometric balance between host-factor surface coverage and the mechanoelastic properties required for nuclear entry.

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Publication Details

Journal
Small
Published
2026-11-01
DOI
https://doi.org/10.1002/smll.76327
Primary Topic
HIV Research and Treatment
Type
article
Field-Weighted Citation Impact
0.00
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Stoichiometric Binding of Cyclophilin‐A to The HIV‐1 Capsid Modulates Its Mechanoelastic Properties (Small 61/2026)

Alexander J. Bryer, Juan S. Rey, Juan R. Perilla
Small
HIV Research and Treatment
article

Stoichiometric Binding of Cyclophilin‐A to The HIV‐1 Capsid Modulates Its Mechanoelastic Properties (Small 61/2026)

Alexander J. Bryer, Juan S. Rey, Juan R. Perilla
article en

Abstract

Nanomechanics The HIV-1 capsid is a protein nanocapsule that must remain stable enough to protect the viral genome while deformable enough to traverse the nuclear pore. In Research Article e75453, Juan R. Perilla and co-workers utilize atomic force microscopy simulations to elucidate how Cyclophilin A binding modulates capsid brittleness, revealing a stoichiometric balance between host-factor surface coverage and the mechanoelastic properties required for nuclear entry.

SmallVol. 22(61)
University of Delaware (US)
Openalex Percentile: Top 14%
HIV Research and Treatment
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