Area of research
Physiology · Molecular Biology
Research interest
Research interests include Chemistry, Biophysics, Amyloid (mycology), Molecular dynamics, Fibril, and Monomer.
Emerging biophysical origins and pathogenic implications of amyloid oligomers
Formation of a β‐Endorphin Corona Mitigates Alzheimer's Amyloidogenesis
Computational insights into the aggregation mechanism of human calcitonin
The Glycine-Rich Region as a Flexible Molecular Glue Promoting hPrP<sub>106–145</sub> Aggregation into β-Sheet Structures
Interpretable Multimodal Deep Ensemble Framework Dissecting Bloodbrain Barrier Permeability with Molecular Features
Computational insights into the cross-talk between medin and A<i>β</i>: implications for age-related vascular risk factors in Alzheimer’s disease
Computational Investigation of Coaggregation and Cross-Seeding between Aβ and hIAPP Underpinning the Cross-Talk in Alzheimer’s Disease and Type 2 Diabetes
Exploring the Impact of Physiological C-Terminal Truncation on α-Synuclein Conformations to Unveil Mechanisms Regulating Pathological Aggregation
Molecular Insights into the Differential Effects of Acetylation on the Aggregation of Tau Microtubule-Binding Repeats
Molecular Insights into the Effects of F16L and F19L Substitutions on the Conformation and Aggregation Dynamics of Human Calcitonin
Uncovering Intermolecular Interactions Driving the Liquid–Liquid Phase Separation of the TDP-43 Low-Complexity Domain via Atomistic Dimerization Simulations
Computational insights into the aggregation mechanism and amyloidogenic core of aortic amyloid medin polypeptide
Co-aggregation of α-synuclein with amyloid-β stabilizes β-sheet-rich oligomers and enhances the formation of β-barrels
Dissecting the Self-assembly Dynamics of Imperfect Repeats in α-Synuclein
Differential Binding and Conformational Dynamics of Tau Microtubule-Binding Repeats with a Preformed Amyloid-β Fibril Seed
SEVI Inhibits Aβ Amyloid Aggregation by Capping the β-Sheet Elongation Edges
Direct Observation of Seeded Conformational Conversion of hIAPP <i>In Silico</i> Reveals the Mechanisms for Morphological Dependence and Asymmetry of Fibril Growth
Deciphering the influence of Y12L and N17H substitutions on the conformation and oligomerization of human calcitonin
Molecular Insights into the Misfolding and Dimerization Dynamics of the Full-Length α-Synuclein from Atomistic Discrete Molecular Dynamics Simulations
Mechanistic insight into the disruption of Tau R3–R4 protofibrils by curcumin and epinephrine: an all-atom molecular dynamics study
Molecular Insights into the Self‐Assembly of Block Copolymer Suckerin Polypeptides into Nanoconfined β‐Sheets
Molecular insights into the oligomerization dynamics and conformations of amyloidogenic and non-amyloidogenic amylin from discrete molecular dynamics simulations
Hydrophobic/Hydrophilic Ratio of Amphiphilic Helix Mimetics Determines the Effects on Islet Amyloid Polypeptide Aggregation
Structural Perturbation of Monomers Determines the Amyloid Aggregation Propensity of Calcitonin Variants
Evidence of Formation of Monolayer Hydrated Salts in Nanopores
Continuous and First-Order Liquid–Solid Phase Transitions in Two-Dimensional Water
Anomalous Phase Behaviors of Monolayer NaCl Aqueous Solutions Induced by Effective Coulombic Interactions within Angstrom-Scale Slits
Spontaneous formation of β-sheet nano-barrels during the early aggregation of Alzheimer’s amyloid beta
Two-dimensional monolayer salt nanostructures can spontaneously aggregate rather than dissolve in dilute aqueous solutions
Misfolding and Self-Assembly Dynamics of Microtubule-Binding Repeats of the Alzheimer-Related Protein Tau