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Synthesis of Thermogelling PolyN-isopropylacrylamide-graft-chondroitin Sulfate Composites with Alginate Microparticles for Tissue Engineering
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Protein Folding Stability and Kinetics in Alginate Hydrogels.

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    Alginate hydrogels stabilize proteins like phosphoglycerate kinase (PGK) by increasing melting temperature. Encapsulation alters protein folding dynamics, affecting unfolding and folding rates, with effects varying by alginate concentration.

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    Force-Clamp Rheometry for Characterizing Protein-based Hydrogels
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    Area of Science:

    • Biophysics
    • Materials Science
    • Biochemistry

    Background:

    • Proteins are frequently encapsulated in alginate gels for applications in drug delivery and tissue engineering.
    • Limited understanding exists regarding how this encapsulation affects intrinsic protein properties, including folding stability and unfolding kinetics.

    Purpose of the Study:

    • To quantitatively assess the impact of alginate hydrogel concentration on the stability and folding dynamics of encapsulated proteins.
    • To investigate the in situ protein unfolding and folding kinetics within alginate hydrogels.

    Main Methods:

    • Utilized fast relaxation imaging (FReI) to monitor protein unfolding in situ within alginate hydrogels.
    • Employed Förster resonance energy transfer (FRET)-labeled phosphoglycerate kinase (PGK) to measure changes in protein folding.
    • Applied temperature jumps to induce unfolding and analyzed FRET response across varying alginate concentrations.

    Main Results:

    • Alginate gels significantly stabilize PGK, increasing its melting temperature by up to 18.4 °C, with stabilization showing a non-monotonic dependence on alginate density.
    • Encapsulation in denser gels caused PGK to deviate more from two-state folding behavior.
    • The gels decreased the unfolding rate and accelerated the folding rate of PGK compared to buffer conditions.

    Conclusions:

    • Alginate gel encapsulation presents both beneficial and detrimental effects on protein folding stability and dynamics.
    • The observed alterations in protein stability and folding kinetics are influenced by alginate concentration and gel density.
    • Phi-value analysis suggests the folding transition state of encapsulated PGK is structurally similar to the folded state, providing insights into potential stabilization mechanisms.