Heteroprotein complex coacervates of ovalbumin and lysozyme: Formation and thermodynamic characterization

Santos, Monique Barreto; Costa, Angélica Ribeiro da; Garcia‐Rojas, Edwin Elard

doi:10.1016/j.ijbiomac.2017.08.132

Cited by 37 publications

(7 citation statements)

References 41 publications

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“…The thermodynamic process of coacervation is still a controversial topic ( Singh and Yethiraj, 2020 ). Garcia-Rojas et al claimed that coacervates containing ovalbumin and lysozyme had two steps of formation, including enthalpically favorable and entropically unfavorable contributions ( Santos et al, 2018 ). The isothermal titration calorimetry data demonstrated that electronic interactions and hydrogen bonds both contributed to the interaction.…”

Section: Mechanism Of Coacervationmentioning

confidence: 99%

Peptide-based coacervates in therapeutic applications

Fang

Wang

2023

Front. Bioeng. Biotechnol.

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Coacervates are droplets formed by liquid‒liquid phase separation. An increasing number of studies have reported that coacervates play an important role in living cells, such as in the generation of membraneless organelles, and peptides contribute to condensate droplet formation. Peptides with versatile functional groups and special secondary structures, including α-helices, β-sheets and intrinsically disordered regions, provide novel insights into coacervation, such as biomimetic protocells, neurodegenerative diseases, modulations of signal transmission, and drug delivery systems. In this review, we introduce different types of peptide-based coacervates and the principles of their interactions. Additionally, we summarize the thermodynamic and kinetic mechanisms of peptide-based coacervates and the associated factors, including salt, pH, and temperature, affecting the phase separation process. We illustrate recent studies on modulating the functions of peptide-based coacervates applied in biological diseases. Finally, we propose their promising broad applications and describe the challenges of peptide-based coacervates in the future.

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Section: Mechanism Of Coacervationmentioning

confidence: 99%

Peptide-based coacervates in therapeutic applications

Fang

Wang

2023

Front. Bioeng. Biotechnol.

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“…The formation of LLPS containing lysozyme and ovalbumin was performed according to previous reports (Santos et al 2018;Iwashita et al 2018), with a few modifications. In the first experiment, a lysozyme solution (#mg/mL in water) and an ovalbumin solution (#mg/mL in water) were mixed 1:1 ratio in water (final concentration is 2.5 mg/mL each).…”

Section: Llps Formation By Mixing Lysozyme and Ovalbuminmentioning

confidence: 99%

“…Lysozyme forms LLPS by adding a high concentration of salt or by mixing with ovalbumin (Taratuta et al 1990;Muschol and Rosenberger 1997;Dumetz et al 2008;Santos et al 2018;Iwashita et al 2018;Bye and Curtis 2019). Therefore, in the present study, we studied the effect of taurine on LLPS formation of lysozyme.…”

Section: Introductionmentioning

confidence: 98%

Taurine suppresses liquid–liquid phase separation of lysozyme protein

et al. 2021

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Taurine is a compatible osmolyte that infers stability to proteins. Recent studies have revealed that liquid-liquid phase separation (LLPS) of proteins underlie the formation of membraneless organelles in cells. In the present study, we evaluated the role of taurine on LLPS of hen egg lysozyme. We demonstrated that taurine decreases the turbidity of the polyethylene glycol-induced crowding solution of lysozyme. We also demonstrated that taurine attenuates LLPS-dependent cloudiness of lysozyme solution with 0.5 or 1M NaCl at a critical temperature. Moreover, we observed that taurine inhibits LLPS formation of a heteroprotein mix solution of lysozyme and ovalbumin. These data indicate that taurine can modulate the formation of LLPS of proteins..

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“…The interactions between DNA and lysozyme have been investigated by various techniques such as atomic force microscopy [ 26 ], optical microscopy [ 27 ], interferometry [ 28 ], small angle X-ray scattering, and light scattering technique [ 29 ]. It was suggested that electrostatic and/or hydrophobic interactions between lysozyme units are important factors driving phase separation in DNA–lysozyme systems [ 1 , 30 ]. There are strong indications that direct interactions between the protein units and the electrostatic attraction between DNA and lysozyme are instrumental in controlling the morphology of the formed assemblies [ 10 , 11 , 12 ].…”

Section: Introductionmentioning

confidence: 99%

DNA–Lysozyme Nanoarchitectonics: Quantitative Investigation on Charge Inversion and Compaction

2022

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The interaction between DNA and proteins is fundamentally important not only for basic research in biology, but also for potential applications in nanotechnology. In the present study, the complexes formed by λ DNA and lysozyme in a dilute aqueous solution have been investigated using magnetic tweezers (MT), dynamic light scattering (DLS), and atomic force microscopy (AFM). We found that lysozyme induced DNA charge inversion by measuring its electrophoretic mobility by DLS. Lysozyme is very effective at neutralizing the positive charge of DNA, and its critical charge ration to induce charge inversion in solution is only 2.26. We infer that the high efficiency of charge neutralization is due to the highly positively charged (+8 e) and compact structure of lysozyme. When increasing the concentration of lysozymes from 6 ng·µL−1 to 70 ng·µL−1, DNA mobility (at fixed concentration of 2 ng·µL−1) increases from −2.8 to 1.5 (in unit of 10−4 cm2·V−1·S), implying that the effective charge of DNA switches its sign from negative to positive in the process. The corresponding condensing force increased from 0 pN to its maximal value of about 10.7 pN at concentrations of lysozyme at 25 ng·µL−1, then decreases gradually to 3.8 pN at 200 ng·µL−1. The maximal condensing force occurs at the complete DNA charge neutralization point. The corresponding morphology of DNA–lysozyme complex changes from loosely extensible chains to compact globule, and finally to less compact flower-like structure due to the change of attached lysozyme particles as observed by AFM.

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Heteroprotein complex coacervates of ovalbumin and lysozyme: Formation and thermodynamic characterization

Cited by 37 publications

References 41 publications

Peptide-based coacervates in therapeutic applications

Peptide-based coacervates in therapeutic applications

Taurine suppresses liquid–liquid phase separation of lysozyme protein

DNA–Lysozyme Nanoarchitectonics: Quantitative Investigation on Charge Inversion and Compaction

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