Sungsoo Na
Korea University · 工学
研究室紹介
Professor Sungsoo Na's research lab specializes in the mechanobiology of cellular systems, focusing on how mechanical forces and structural proteins regulate cell behavior and disease progression. The lab investigates the mechanical properties of key cytoskeletal and extracellular matrix proteins such as plectin and amyloid fibrils, exploring their roles in cellular stiffness, force transmission, and disease-related aggregation. Using advanced techniques like FRET-based biosensors and nanomechanical probing, the lab uncovers how protein conformational changes and self-assembly processes underlie both physiological functions and pathological conditions such as neurodegeneration. The research bridges molecular biophysics with cell mechanics, emphasizing the structure-function relationships in mechanically robust biomolecular assemblies.
Research Overview
Research Output Trend
Figures are computed from collected data and may differ slightly.
Selected Papers
15It is widely postulated that mechanotransduction is initiated at the local force-membrane interface by inducing local conformational changes of proteins, similar to soluble ligand-induced signal transduction. However, all published reports are limited in time scale to address this fundamental issue. Using a FRET-based cytosolic Src reporter in a living cell, we quantified changes of Src activities as a local stress via activated integrins was applied. The stress induced rapid (<0.3 s) activation
Plectin is a 500-kDa cross-linking protein that plays important roles in a number of cell functions including migration and wound healing. We set out to characterize the role of plectin in mechanical properties of living cells. Plectin(-/-) cells were less stiff than plectin(+/+) cells, but the slopes of the two power laws in response to loading frequencies (0.002-1,000 Hz) were similar. Plectin(-/-) cells lost the capacity to propagate mechanical stresses to long distances in the cytoplasm; tra
Abstract Recent experimental studies have shown that amyloid fibril formed by aggregation of β peptide exhibits excellent mechanical properties comparable to other protein materials such as actin filaments and microtubules. These excellent mechanical properties of amyloid fibrils are related to their functional role in disease expression. This indicates the necessity of understanding how an amyloid fibril achieves the remarkable mechanical properties through self‐aggregation with structural hier
Amyloid fibrils playing a critical role in disease expression, have recently been found to exhibit the excellent mechanical properties such as elastic modulus in the order of 10 GPa, which is comparable to that of other mechanical proteins such as microtubule, actin filament, and spider silk. These remarkable mechanical properties of amyloid fibrils are correlated with their functional role in disease expression. This suggests the importance in understanding how these excellent mechanical proper
A study of the vibration control of cantilevers exposed to blast loading is presented. Whereas the structure used in this analysis is in the form of a thin-walled beam of closed cross-section contour, the control is based upon the simultaneous implementation of adaptive materials technology and of optimal feedback control. Issues related to the the influence upon dynamic response of size and location along the beam span of piezoactuator patches are investigated, and the efficiency of this combin
Amyloid β (Aβ) aggregates, which are a hallmark for neurodegenerative disease, are formed through a self-assembly process such as aggregation of Aβ peptide chains. This aggregation process depends on the solvent conditions under which the proteins are aggregated. Nevertheless, the underlying mechanism of the ionic effect on the formation and stability of amyloid aggregates has not been fully understood. Here, we report how metal ions play a role in the formation and stability of Aβ aggregates at
The coarse-grained structural model such as Gaussian network has played a vital role in the normal mode studies for understanding protein dynamics related to biological functions. However, for the large proteins, the Gaussian network model is computationally unfavorable for diagonalization of Hessian (stiffness) matrix for the normal mode studies. In this article, we provide the coarse-graining method, referred to as "dynamic model condensation," which enables the further coarse-graining of prot
Spider and silkworm silk proteins have received much attention owing to their inherent structural stability, biodegradability, and biocompatibility. These silk protein materials have various mechanical characteristics such as elastic modulus, ultimate strength and fracture toughness. While the considerable mechanical characteristics of the core crystalline regions of spider silk proteins at the atomistic scale have been investigated through several experimental techniques and computational studi