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Research Center for Bioconvergence Analysis

Research Center for Bioconvergence Analysis Analytical Science > Major Research Activities Home

The Research Center for Bioconvergence Analysis is devoted to the development and application of biotechnology with the ultimate goal of discovering how biological systems operate. Research efforts are focused on the establishment of integrated analytical platforms and the support of collaborators involved in joint research in the field of disease diagnosis and therapy. A significant contribution has been made to solving problems which are significant in the nation and in society.

Main Research Field

Development of an integrated analysis system for studying diseases resulting from protein amyloidosis

  • Development of an integrated biophysical analysis system for the study of the molecular mechanisms of protein amyloidosis
  • Development of an integrated bioimaging analysis system to diagnose amyloidosis-related diseases and to evaluate the effects of drug treatment on these diseases

Development of a multi-omics big data convergence platform

  • Development of a multi-omics big data open platform based on advanced research infrastructure for the implementation of precision medicine
  • Construction of a proteomic/metabolomic/phenotypic database and data portal operation
  • Development of standard analytic techniques for multi-omics and their utilization in research

Convergence research

  • Mass spectrometry based validation of glycan-humanized model mouse (Collaborators: KRIBB/KBSI)
  • Development of low-toxicity anticancer therapeutics based on epi-proteome (Collaborators: KRIBB/KIST/KBSI)
  • Virus surveillance and diagnosis research (Collaborators: KRICT/KBSI/KIT)
  • Bio-luminescent image-monitoring of anti-cancer efficacy of CAR-NK cell therapy (Collaborators: KRIBB/KBSI/KIT/SNU/KIST/KBIO/SKKU)

Representative Research Cases

Diverse structural conversion and aggregation pathways of Alzheimerʼs Amyloid-β (1–40)

  • Protein aggregation such as amyloid formation and oligomerization has shown to be a generic property of polypeptide chains and to cause several hundreds of diseases including Alzheimer‘s and Parkinson’s diseases as well as type 2 diabetes. Pathways of protein aggregation depend largely on structures of monomers and environment conditions.
  • Diverse structural conversion and aggregation pathways of Alzheimerʼs Amyloid-β (1-40)Diverse structural conversion and aggregation pathways of Alzheimerʼs Amyloid-β (1-40)

Molecular architecture of a cylindrical self-assembly at human centrosomes

  • Two human pericentriolar material scaffolds, Cep63 and Cep152, cooperatively generate a heterotetrameric α-helical bundle that functions in conjunction with its neighboring hydrophobic motifs to self-assemble into a higher-order cylindrical architecture capable of recruiting downstream components, including Plk4, a key regulator for centriole duplication (Nature communication 2019, 10(1), 1151)
  • Crystal structure of the Cep63 and Cep152 complex forming an antiparallel four-helix bundleCrystal structure of the Cep63 and Cep152 complex forming an antiparallel four-helix bundle

Syringeable immunotherapeutic nanogel reshapes tumor microenvironment and prevents tumor metastasis and recurrence

  • Develop a syringeable immunomodulatory multidomain nanogel(iGel). Local and extended release of immunomodulatory drugs from iGel deplete immunosuppressive cells, while inducing immunogenic cell death and increased immunogenicity. (Nature communication, 2019, 10, 3745)
  • Schematic iGel for the prevention of tumor recurrence and metastasisSchematic iGel for the prevention of tumor recurrence and metastasis