A5101950988- Protein Structure and Dynamics
- Enzyme Structure and Function
- Alzheimer's disease research and treatments
- Protein Interaction Studies and Fluorescence Analysis
- Advanced Fluorescence Microscopy Techniques
- Metabolomics and Mass Spectrometry Studies
- Protein purification and stability
- Proteins in Food Systems
- Epigenetics and DNA Methylation
- Infant Nutrition and Health
- Melanoma and MAPK Pathways
- Bacteriophages and microbial interactions
- Lipid Membrane Structure and Behavior
- Supramolecular Self-Assembly in Materials
- Pickering emulsions and particle stabilization
- Cancer-related gene regulation
- Enzyme function and inhibition
- Protein Hydrolysis and Bioactive Peptides
- Surfactants and Colloidal Systems
- Nanoparticle-Based Drug Delivery
- Biotin and Related Studies
- Computational Drug Discovery Methods
University of Copenhagen
2021-2024
North Minzu University
2018
University of Chinese Academy of Sciences
2017
Jiangsu University
2017
Jintan People's Hospital
2017
Amyloid aggregation is associated with many diseases and may also occur in therapeutic protein formulations. Addition of co-solutes a key strategy to modulate the stability proteins pharmaceutical formulations select inhibitors for drug design context diseases. However, heterogeneous nature this multicomponent system terms structures mechanisms poses number challenges analysis chemical reaction. Using insulin as polysorbate 80 co-solute, we combine spatially resolved fluorescence approach...
De novo designed protein supramolecular structures are nowadays attracting much interest as highly performing biomaterials. While a clear advantage is provided by the intrinsic biocompatibility and biodegradability of peptide building blocks, developing sustainable green bottom up approaches for finely tuning material properties still remains challenge. Here, we present an experimental study on formation microparticles in form particulates from α-lactalbumin using bulk mixing water solution...
Protein misfolding in the form of fibrils or spherulites is involved a spectrum pathological abnormalities. Our current understanding protein aggregation mechanisms has primarily relied on use spectrometric methods to determine average growth rates and diffraction-limited microscopes with low temporal resolution observe large-scale morphologies intermediates. We developed REal-time kinetics via binding Photobleaching LOcalization Microscopy (REPLOM) super-resolution method directly quantify...
To understand how the stabilities of key nuclei fragments affect protein folding dynamics, we simulate by molecular dynamics (MD) simulation in aqueous solution four cut out a G, including one α-helix (seqB: KVFKQYAN), two β-turns (seqA: LNGKTLKG and seqC: YDDATKTF), β-strand (seqD: DGEWTYDD). The Markov State Model clustering method combined with coarse-grained conformation letters are employed to analyze data sampled from 2-μs equilibrium MD trajectories. We find that seqA seqB have more...
Abstract Protein misfolding in the form of fibrils or spherulites is involved a spectrum pathological abnormalities. Our current understanding protein aggregation mechanisms has primarily relied on use spectrometric methods to determine average growth rates and diffraction-limited microscopes with low temporal resolution observe large-scale morphologies intermediates. We developed REal-time kinetics via binding Photobleaching LOcalisation Microscopy (REPLOM) super-resolution method directly...
Abstract The misfolding of proteins and their aggregation in the form fibrils or amyloid-like spherulites are involved a spectrum pathological abnormalities. Our current understanding protein amyloid mechanisms has primarily relied on use spectrometric methods to determine average growth rates diffraction limited microscopes with low temporal resolution observe large-scale morphologies intermediates. We developed REal-time kinetics via binding Photobleaching LOcalisation Microscopy ( REPLOM...
Protein arginine methyltransferase 1 (PRMT1) forms S-adenosylhomocysteine (SAH) and by transferring methyl of SAM(S-adenosyl-L-methionine) to the substrate arginine, then various effects in vivo occur.Our research group designed synthesized 28 PRMT1 inhibitors which take furan ring as mother nucleus earlier stage, this selected five representative composite classical known inhibitor AMI1 for 100 nanoseconds molecular dynamics simulations explore binding modes these compounds.The found that...
ABSTRACT Amyloid aggregation is associated with many diseases and may also occur in therapeutic protein formulations. Addition of co-solutes a key strategy to modulate the stability proteins pharmaceutical formulations select inhibitors for drug design context diseases. However, heterogeneous nature this multi-component system terms structures mechanisms poses number challenges analysis chemical reaction. Combining spatially resolved fluorescence approach single molecule microscopy machine...
Abstract Amyloid protein aggregates are not only associated with neurodegenerative diseases and may also occur as unwanted by-products in protein-based therapeutics. Surfactants often employed to stabilize formulations reduce the risk of aggregation. However, surfactants alter protein-protein interactions thus modulate physicochemical characteristics any formed. Human insulin aggregation was induced at low pH presence varying concentrations surfactant polysorbate 80. Various spectroscopic...
Abstract The misfolding of proteins and their aggregation in the form fibrils or amyloid-like spherulites are involved a spectrum degenerative diseases. Our current understanding protein mechanisms has primarily relied on use conventional spectrometric methods to determine average growth rates microscopic morphology final structures, consequently masking morphological heterogeneity aggregates. We developed REal-time kinetics via binding Photobleaching LOcalisation Microscopy (REPLOM)...