IN THE MEDIA
Trypsin adsorption.movDecorated nanoparticles prevent allergic reactions [link]
Adaptive PPSU nanoparticles enable protein adsorption while preserving the enzymatic activity
Water layer lubricates the protein-nanoparticle interface
Microporous water with high gas solubilities [link]
Proteins stabilize microporous zeolite and MOF in water
Gas capture was highly elevated
Proteolytic Stability of Peptide-Brush Polymers [link]
PBPs display globular morphology
The proteolytic stability of PBPs is associated with the hydrophobicity of PBP backbones
Research Exposes New Vulnerability in SARS-CoV-2 [link]
The polybasic cleavage sites are around 10 nm from the RBD-ACE2 interface
They likely increase viral infection (experimentally validated later)
A model peptide remarkably neutralized the polybasic cleavage sites
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Selected to be one of the significant scientific events in 2020 in Wikipedia
Researchers Find Enzymes Naturally Select their Own Polymer Sequences [link]
Distinct domain exist at protein surfaces
Protein surface domain selectively adsorb amphiphilic polymers
Like a fishing net’, nanonet collapses to trap drug molecules [link]
In collaboration with Prof. Evan Scott's group, we designed a new polymer PPSU
PPSU displayed exceptionally high encapsulation efficiency of proteins, DNA, RNA, and polar small molecules, which used to be highly challenging owing to their water solubility
Discovery Makes It Easier to Design Synthetic Proteins that Rival their Natural Counterparts [link]
The random heteropolymes form transmembrane structure
The transmembrane polymers are structurally and functionally similar to transmembrane proteins in selectively and efficiently transporting proton ions
Researchers find way to keep proteins functioning outside of the cell [link]
In collaboration with Prof. Ting Xu's group at UC Berkeley, we designed random heteropolymers
The random heteropolymer can preserve protein activity in non-aqueous conditions
Atomistic simulations found core (protein) - shell (polymer) structures
Polar protein surface domains selective adsorb polar components of the random heteropolymers