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Hameed, H. A.

Publications and source records attributed to Hameed, H. A..

2 recordsLinked to original sources

Inter-lamin interactions control meshwork topologyin a polymer-gel model of nuclear lamina

The nuclear lamina is a specialized two-dimensional filamentous polymer meshwork that provides structural integrity and elasticity to the nucleus while orchestrating diverse cellular processes. Composed of interacting A- and B-type lamin networks, this structure undergoes tightly regulated self-assembly that is frequently perturbed by disease-causing mutations such as those observed in laminopathies or cardiomyopathies. However, because filament assembly, peripheral adsorption of lamins, and network branching occur concurrently in vivo, isolating the specific biophysical parameters that dictate emergent lamina topology has remained a major challenge. Here, we present a polymer-physics approach that explicitly resolves the spontaneous self-assembly of lamin networks under nuclear confinement. By modeling lamin dimers as semiflexible filaments with distinct interactive domains, we demonstrate that the formation of continuous, high-aspect-ratio fibers strictly requires a coordination cascade of parallel lateral alignment sites and longitudinal head-to-tail interactions between lamins. We show that the thermodynamic affinity between lamin-A and the peripheral boundary (i.e., the inner nuclear membrane and lamin B network) acts as a kinetic switch: weak surface adsorption drives network phase separation and large lamin-free gaps, whereas robust substrate binding stabilizes highly branched networks with uniform lamin distribution. Finally, uniaxial compression simulations reveal that mutations altering these molecular binding interfaces severely compromise macroscale nuclear load-bearing capacity and induce structural vulnerabilities. Collectively, our model establishes a predictive, multi-scale view that directly bridges nanoscale lamin interactions with mesoscale topological remodeling of lamina and macroscale nuclear mechanopathology.

biophysics↗

Exploring Nuclear Lamina Structure and Lamin Dissociation in Progeria through Polymer Modeling

One of the key structural proteins in the eukaryotic cell nucleus is lamin. Lamins can assemble into a two-dimensional protein meshwork at the nuclear periphery, referred to as the nuclear lamina, which provides rigidity and shape to the nucleus. Mutations in lamin proteins that affect the structure of the nuclear lamina underlie laminopathic diseases, including Hutchinson-Gilford Progeria Syndrome (HGPS). Experiments have shown that, compared to healthy cells, lamin supramolecular structures (e.g., protofilaments) assemble into a thicker lamina structure in HGPS, where lamins form highly stable nematic microdomains at the nuclear periphery, reminiscent of liquid crystals. This significantly alters the morphological and mechanical properties of the nucleus. In this study, we investigate the aggregation of lamin fibrous structures and their dissociation kinetics from the nuclear periphery by modeling them as coarse-grained, rod-like polymer chains confined in a rigid spherical shell. Our model recapitulates the formation of multidirectional nematic domains at the nuclear surface and the reduced lamin dissociation observed in HGPS nuclei by adjusting lamin concentration, lamin-lamin (specifically head-tail), and lamin-shell association strengths. While nematic phase formation requires relatively strong lamin-shell affinity under any non-vanishing inter-lamin attraction, the thickness of this layer is primarily controlled by head-tail association strength in the model. Furthermore, the dissociation kinetics of lamin chains from the chain aggregates at the periphery (lamina) exhibits a concentration-dependent dissociation (facilitated dissociation) pattern governed by weak lamin-lamin interactions, reminiscent of healthy nuclei. Overall, our calculations demonstrate how an interplay between molecular interactions altered by mutations and lamin concentration can lead to an abnormal nuclear lamina in laminopathic diseases.

biophysics↗