Longfu Xu

Longfu Xu

PhD in Biophysics

Vrije Universiteit Amsterdam

Biography

  • 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.
Interests
  • Single Molecule Biophysics
  • DNA-Protein Interaction
  • Single-molecule Visua- & Manipulation
Education
  • PhD in BioPhysics, 2022(expected)

    Vrije Universiteit Amsterdam

  • Msc in Biochemical Engineering, 2017

    University of Chinese Academy of Sciences

  • BSc in Food Science, 2014

    Northeast Agricultural University

Experience

 
 
 
 
 
Vrije Universiteit Amsterdam
PhD in Biophysics
Oct 2017 – Present Amsterdam

PhD Projects include:

  • Grab, manipulate and watch single DNA molecule replication
  • Direct watching DNAp removes SSB during replication
  • Single-molecule studies of the effect of Mg2+on replication and exonuclease activity by DNA
  • Quantifying how protein affects DNA melting within replisome under tension
 
 
 
 
 
University of Chinese Academy of Sciences
Master Student in Biochemical Engineering
Sep 2014 – Jul 2017 Beijing

Msc. Projects include:

  • Development of thiol-specific PEGylation reagents aiming for elongating protein half-life based on catechol-derivatives.
  • Purification and characterization of a long-acting ciliary neurotrophic factor via genetically fused with an albumin-binding domain

Projects

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Purification and characterization of a long-acting ciliary neurotrophic factor via genetically fused with an albumin-binding domain
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.
Purification and characterization of a long-acting ciliary neurotrophic factor via genetically fused with an albumin-binding domain
Development of thiol-specific PEGylation reagents aiming for elongating protein half-life based on catechol-derivatives
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.
Development of thiol-specific PEGylation reagents aiming for elongating protein half-life based on catechol-derivatives
Single DNA molecule sequencing
We develop a method to fast sequence a single DNA molecule, which can be further used for virus detection.
Single DNA molecule sequencing
Quantifying how protein affects DNA melting within replisome under tension
We used a machanical model to quantify how protein affects DNA melting within replisome under tension.
Quantifying how protein affects DNA melting within replisome under tension
Watching DNAp removes SSB during replication
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.
Watching DNAp removes SSB during replication

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