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Biology subjects

Stellato, M.

Publications and source records attributed to Stellato, M..

2 recordsLinked to original sources

Spheroid surgery: a first-generation micromanipulation platform for extracting viable cell clusters from the outer layers of hydrogel-embedded spheroids

Three-dimensional (3D) cell culture systems have gained attention as in vitro models capable of reproducing the tissue-like architecture, spatial organization, and physiological morphology of in vivo tumors. Their ability to mimic native cell-cell and cell-matrix interactions has positioned 3D cell cultures as powerful models for studying tumor biology and drug responses. However, methods for the localized extraction of viable cells remain limited, as existing approaches often disrupt the original 3D structure, limit access to defined regions, or compromise cell viability, restricting the biological insight that can be achieved. We present a manual, micropipette-based manipulation system designed to extract viable multicellular clusters from the outer layers of compact 3D tumor spheroids, embedded in biocompatible hydrogels. The extracted clusters remained fully functional, demonstrating that the procedure is sufficiently gentle to remove small multicellular units. This technology enables the localized extraction of viable multicellular clusters from 3D in vitro models without complete dissociation of the parent spheroid. The method opens new opportunities for longitudinal studies, spatially targeted sampling and controlled manipulation of living 3D cultures. This capability marks a step toward a new era of 3D model manipulation, where researchers can add, remove, or replace specific regions of living multicellular systems with precision.

bioengineering↗

Structural characterization of the antimicrobial peptides myxinidin and WMR in bacterial membrane mimetic micelles and bicelles

Antimicrobial peptides are a promising class of alternative antibiotics that interact selectively with negatively charged lipid bilayers. This paper presents the structural characterization of the antimicrobial peptides myxinidin and WMR associated with bacterial membrane mimetic micelles and bicelles by NMR, CD spectroscopy, and Molecular Dynamics simulations. Both peptides adopt a different conformation in the lipidic environment than in aqueous solution. The location of peptides in micelles and bicelles has been studied by paramagnetic relaxation enhancement experiments with paramagnetic tagged 5- and 16-doxyl stearic acid (5-/16-SASL). Multi-microsecond long molecular dynamics simulations of multiple copies of the peptides were used to gain an atomic level of detail on membrane-peptide and peptide-peptide interactions. Our results highlight an essential role of the negatively charged membrane mimetic in the structural stability of both myxinidin and WMR. The peptides localize predominantly in the membranes headgroup region and have a noticeable membrane thinning effect on the overall bilayer structure. Myxinidin and WMR show different tendency to selfaggregate, which is also influenced by the membrane composition (DOPE/DOPG versus DOPE/DOPG/CL) and can be related to the previously observed difference in the ability of the peptides to disrupt different types of model membranes.

biochemistry↗