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Advancing Protein Stability and Biophysical Characterization

  • Mariana Carvalho S. do Nascimento
  • Jul 29
  • 2 min read

The Uncle™ platform combines high-throughput thermal stability analysis by nano Differential Scanning Fluorimetry (nanoDSF), Dynamic Light Scattering (DLS), and Static Light Scattering (SLS), into a single, powerful instrument, enabling rapid and comprehensive protein characterization. With the ability to analyze up to 48 samples simultaneously using only microliter volumes, Uncle delivers detailed insights into protein unfolding, conformational stability, aggregation, and intermolecular interactions. This accelerates biomolecular research while substantially reducing sample consumption.


Protein stability is a critical parameter in the development of enzymes, therapeutic proteins, vaccines, and other biologics. Even subtle structural changes can compromise protein function, shorten shelf life, or promote aggregation, ultimately impacting both efficacy and safety. The Uncle platform allows researchers to evaluate these properties with exceptional sensitivity, enabling rapid screening of multiple protein variants, buffer conditions, and formulations in a fraction of the time required by conventional techniques.


Beyond stability analysis, the integration of nanoDSF with Dynamic and Static Light Scattering provides complementary data on aggregation propensity, particle size distribution, and structural transitions during thermal unfolding. Together, these measurements generate a comprehensive biophysical profile of proteins, supporting applications ranging from protein engineering, formulation optimization, quality control, and drug discovery, including the investigation of protein–ligand interactions.


As an example, in our laboratory, the Uncle platform plays an essential role in the characterization of L‑asparaginase, a therapeutic enzyme essential in the treatment of Acute Lymphoblastic Leukemia (ALL), the most common pediatric cancer. By monitoring the conformational stability and aggregation behavior of different variations of this enzyme, under various experimental conditions, we have been gaining valuable insights that contribute to the development of more stable, effective, and accessible biopharmaceutical presentations. Beyond this, the technology supports a broad range of structural biology and biotechnology projects, reinforcing our commitment to translating fundamental protein science into innovative solutions in the fields of therapy, diagnostics, food additives, and technical enzymes.

 
 
 

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