Exploring the Origins of Association of Poly(acrylic acid) Polyelectrolyte with Lysozyme in Aqueous Environment through Molecular Simulations and Experiments

Author:

Arnittali Maria123,Tegopoulos Sokratis N.4ORCID,Kyritsis Apostolos4,Harmandaris Vagelis123ORCID,Papagiannopoulos Aristeidis5ORCID,Rissanou Anastassia N.5ORCID

Affiliation:

1. Institute of Applied and Computational Mathematics, Foundation for Research and Technology Hellas, IACM/FORTH, GR-71110 Heraklion, Greece

2. Department of Mathematics and Applied Mathematics, University of Crete, GR-71409 Heraklion, Greece

3. Computation-Based Science and Technology Research Center, The Cyprus Institute, Nicosia 2121, Cyprus

4. School of Applied Mathematical and Physical Sciences, National Technical University of Athens, GR-15772 Athens, Greece

5. Theoretical & Physical Chemistry Institute, National Hellenic Research Foundation, 48 Vassileos Constantinou Avenue, GR-11635 Athens, Greece

Abstract

This study provides a detailed picture of how a protein (lysozyme) complexes with a poly(acrylic acid) polyelectrolyte (PAA) in water at the atomic level using a combination of all-atom molecular dynamics simulations and experiments. The effect of PAA and temperature on the protein’s structure is explored. The simulations reveal that a lysozyme’s structure is relatively stable except from local conformational changes induced by the presence of PAA and temperature increase. The effect of a specific thermal treatment on the complexation process is investigated, revealing both structural and energetic changes. Certain types of secondary structures (i.e., α-helix) are found to undergo a partially irreversible shift upon thermal treatment, which aligns qualitatively with experimental observations. This uncovers the origins of thermally induced aggregation of lysozyme with PAA and points to new PAA/lysozyme bonds that are formed and potentially enhance the stability in the complexes. As the temperature changes, distinct amino acids are found to exhibit the closest proximity to PAA, resulting into different PAA/lysozyme interactions; consequently, a different complexation pathway is followed. Energy calculations reveal the dominant role of electrostatic interactions. This detailed information can be useful for designing new biopolymer/protein materials and understanding protein function under immobilization of polyelectrolytes and upon mild denaturation processes.

Publisher

MDPI AG

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