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Connecting high-temperature and low-temperature protein stability and aggregation.

Mónica Rosa1, Christopher J Roberts2, Miguel A Rodrigues1

  • 1Centro de Química Estrutural, Department of Chemical Engineering, Instituto Superior Técnico, Universidade de Lisboa, Lisboa, Portugal.

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Cold temperatures can trigger protein aggregation through the same mechanisms as heat. This finding suggests sub-zero temperatures can impact protein stability and shelf life, even without freezing.

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Area of Science:

  • Biochemistry
  • Protein Science
  • Physical Chemistry

Background:

  • Protein aggregation poses challenges for protein preservation in labs and industry.
  • High temperatures accelerate aggregation by promoting unfolded protein states.
  • The relevance of these mechanisms for low-temperature (cold) aggregation remains unclear.

Purpose of the Study:

  • To directly compare protein aggregation kinetics and thermodynamics under heat and cold stress.
  • To investigate if identical mechanisms drive aggregation across a wide temperature range.
  • To utilize bovine hemoglobin as a model system for this investigation.

Main Methods:

  • Comparative analysis of aggregation kinetics at high and low temperatures.
  • Determination of folding/unfolding thermodynamics for bovine hemoglobin.
  • Exploration of aggregation temperature-of-maximum-stability.

Main Results:

  • The study found that the same non-native aggregation mechanism operates from high to low temperatures.
  • An aggregation temperature-of-maximum-stability was identified slightly below 0°C.
  • Sub-zero temperatures induce cold-mediated aggregation, independent of freezing.

Conclusions:

  • Cold stress can induce protein aggregation via mechanisms similar to heat stress.
  • Sub-zero temperatures are critical for understanding protein stability and shelf-life.
  • Cold-stress studies offer a potential alternative to heat-stress for predicting protein stability.