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Updated: May 14, 2026

Tracking Single Proteins in Lipid Bilayers Using Fluorescence Microscopy
Published on: December 12, 2025
In silico study of human aquaporin AQP11 and AQP12 channels
Luisa Calvanese1, Marialuisa Pellegrini-Calace, Romina Oliva
1Department of Applied Sciences, University Parthenope of Naples, Centro Direzionale Isola C4, Naples I-80143, Italy.
Abstract:
AQP11 and AQP12 are the most distantly related paralogs of the aquaporin family in human. They share indeed a low sequence similarity with other aquaporins and exhibit a modified N-terminal NPA signature motif. Furthermore, they have an anomalous subcellular localization. The AQP11 and AQP12 biological role remains to be fully clarified and their ability to allow transport of water is still debated. We have built accurate 3D-models for AQP11 and AQP12 and comprehensively compared their sequence and structure to other known aquaporins. In order to investigate whether they appear compatible or not with water permeability, we especially focused on the amino acid composition and electrostatics of their channels, keeping the structure of the low-water efficiency AQP0 as a reference system. Our analysis points out a possible alternative ar/R site and shows that these aquaporins feature unique residues at key pore-lining positions that make the shape, composition and electrostatics of their channel peculiar. Such residues can represent pivotal hints to study and explain the AQP11 and AQP12 biological and molecular function.
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