An experienced biophysical and biochemical researcher with a big passion for understanding life with physical principles.
Currently, working as a PhD candidate in the laboratory of Gijs Wuite at Vrije Universiteit Amsterdam, focusing on DNA-protein interaction with single-molecule manipulation & visualization tools.
Hold a Master of Science (M.Sc.) Degree from University of Chinese Academy of Science, focusing on the long-acting strategy of biopharmaceuticals, e.g.: PEGylation or albumin-binding domain fused protein.
Ciliary neurotrophic factor (CNTF) is a promising candidate for the
treatment of neurodegenerative or metabolic diseases, but suffers rapid
clearance in body. Here in this project, we constructed a new long-acting recombinant human
CNTF (rhCNTF) by genetic fusion with an albumin-binding domain (ABD) through a
flexible peptide linker, hoping to endow the new molecule prolonged serum
circulation time by binding with endogenous human serum albumin (HSA) and then
utilizing the naturally long-half-life property of HSA.
In this project, we described a new thiol-specific PEGylation strategy based on catechol-derived reactive quinone species. Catechol-derived polyethylene glycol (PEG) was synthesized by coupling linear PEG N-hydroxysuccinimide to dopamine and then oxidized to quinone. PEG-dopaquinone (PEG-DAQ) mostly modifying the free cysteines of two model proteins of truncated flagellin (CBLB502) and recombined human ciliary neurotrophic factor (rhCNTF) evidenced its thiol-specificity.
Transitionally exposed ssDNA during replication are coated
and stabilized by single-stranded DNA binding protein (SSB) within the
replisome. How these SSB protein regulates and are displaced by DNA polymerase
(DNAp) however are still poorly understood. Here T7 DNAp and T7 gp2.5 (SSB)
are used as model proteins to investigate their interaction.