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Pigeon egg white protein-based transparent durable hydrogel via monodisperse ionic surfactant-mediated protein condensation.

ABSTRACT: The thermal gelation property of proteins is useful in creating protein-based materials. The gelation of protein solution often proceeds by the random aggregation of denatured proteins, and the protein-based gels are typically brittle or opaque, or both. Improvement in the mechanical and optical properties of protein-based materials are required for them to be practical and functional. This study investigated pigeon egg white, which is semitransparent in its thermally gelled state, as a protein source for creating hydrogel materials. The protein thermal gelation process was initiated from the orderly condensed state of proteins complexed with monodisperse ionic surfactants to suppress random aggregation. The resultant gel showed transparency in the visible light region and was not destroyed at 99% compression under 17.8 MPa compressive stress, 350-fold higher than the compressive fracture strength of typical boiled pigeon egg white. These results showed that durable transparent hydrogels could be fabricated by the rational combination of natural proteins and surfactants.

SUBMITTER: Zhou X

PROVIDER: S-EPMC8930986 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature

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Pigeon egg white protein-based transparent durable hydrogel via monodisperse ionic surfactant-mediated protein condensation.

Zhou Xinlian X Chen Zaozao Z Nojima Tatsuya T

Scientific reports 20220317 1

The thermal gelation property of proteins is useful in creating protein-based materials. The gelation of protein solution often proceeds by the random aggregation of denatured proteins, and the protein-based gels are typically brittle or opaque, or both. Improvement in the mechanical and optical properties of protein-based materials are required for them to be practical and functional. This study investigated pigeon egg white, which is semitransparent in its thermally gelled state, as a protein ...[more]

PMID: 35301357

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Project description:Proteins with low complexity, disordered sequences are receiving increasing attention due to their central roles in the biogenesis and regulation of membraneless organelles. In eukaryotic organisms, a substantial fraction of disordered proteins reside in the nucleus, thereby facilitating the formation of nuclear bodies, nucleolus, and chromatin compartmentalization. The heterochromatin family of proteins (HP1) is an important player in driving the formation of gene silenced mesoscopic heterochromatin B compartments and pericentric regions. Recent experiments have shown that the HP1a sequence of Drosophila melanogaster can undergo liquid-liquid phase separation under both in vitro and in vivo conditions, induced by changes of the monovalent salt concentration. While the phase separation of HP1a is thought to be the mechanism underlying chromatin compartmentalization, the molecular level mechanistic picture of salt-driven phase separation of HP1a has remained poorly understood. The disordered hinge region of HP1a is seen as the driver of salt-induced condensation because of its charge enriched sequence and post-translational modifications. Here, we set out to decipher the mechanisms of salt-induced condensation of HP1a through a systematic study of salt-dependent conformations of single chains and fuzzy dimers of disordered HP1a hinge sequences. Using multiple independent all-atom simulations with and without enhanced sampling, we carry out detailed characterization of conformational ensembles of disordered HP1a chains under different ionic conditions using various polymeric and structural measures. We show that the mobile ion release, enhancement of local transient secondary structural elements, and side-chain exposure to solvent are robust trends that accompany fuzzy dimer formation. Furthermore, we find that salt-induced changes in the ensemble of conformations of HP1a disordered hinge sequence fine-tune the inter-chain vs. self-chain interactions in ways that favor fuzzy dimer formation under low salt conditions in the agreement with condensation trends seen in experiments.

Dataset Information

Pigeon egg white protein-based transparent durable hydrogel via monodisperse ionic surfactant-mediated protein condensation.

Publications

Pigeon egg white protein-based transparent durable hydrogel via monodisperse ionic surfactant-mediated protein condensation.

Similar Datasets

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