<scp>Peptide‐based</scp>Coacervates: A Biomimetic Protocell

Abbas, Manzar

doi:10.1002/9783527841264.ch12

Peptide Self‐Assembly and Engineering 2024

DOI: 10.1002/9783527841264.ch12

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Peptide‐basedCoacervates: A Biomimetic Protocell

Manzar Abbas

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2024

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Cited by 2 publications

References 41 publications

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Charge‐Mediated Interactions Affect Enzymatic Reactions in Peptide Condensates

Harris,

Berman,

Lampel

2024

ChemSystemsChem

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Biomolecular condensates, formed through liquid‐liquid phase separation (LLPS), serve as enzymatic reaction centers in cells by increasing local concentrations of enzymes and substrates, thereby facilitating reaction kinetics and regulatory mechanisms. Inspired by these natural systems, synthetic condensates are being developed for diverse applications, including payload delivery, sensing, and as microreactors where enzymatic reaction kinetics can be modulated by factors like pH, viscosity, and enzyme‐substrate co‐localization. Here, we investigate how the physicochemical properties of enzymes and substrates influence condensate formation and function as microreactors. Focusing on cellulase and alkaline phosphatase, which differ in molecular weight and isoelectric point, we employed a minimalistic complex coacervation system of oppositely charged LLPS‐promoting peptides. Our findings show how electrostatic forces within condensates influence their role as microreactors. Specifically, the ability of condensates to encapsulate or exclude phosphatase and cellulase and their substrates, which is pivotal for the regulation of reaction kinetics, is determined by the enzyme surface charge, substrate charge, and condensate charge stoichiometry. These results highlight the potential of utilizing electrostatic forces within condensates to modulate enzymatic reactions, providing critical insights for developing synthetic condensates as microreactors in biotechnology and materials science.

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Charge‐Mediated Interactions Affect Enzymatic Reactions in Peptide Condensates

Harris,

Berman,

Lampel

2024

ChemSystemsChem

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Engineering of self-assembled silver-peptide colloidal nanohybrids with enhanced biocompatibility and antibacterial activity

Saeed,

Atiq,

Rafiq

et al. 2024

Sci Rep

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Several bacterial strains have developed resistance against commercial antibiotics, and interestingly, supramolecular nanomaterials have shown considerable advantages for antibacterial applications. However, the main challenges in adopting nanotechnology for antibacterial studies are random aggregation, compromised toxicity, multi-step preparation approaches, and unclear structure-function properties. Herein, we designed the amphiphilic tripeptide that acts as a reducing and capping agent for silver metal to form silver-peptide colloidal nanohybrids with the mild assistance of UV light (254 nm) through the photochemical reduction method. The nanohybrids are characterized by different spectroscopic and microscopic techniques, and non-covalent molecular interactions between metal and peptide building blocks confirm their central role in the formation of nanohybrids. The tripeptide is biocompatible and can reduce the toxicity of silver ions (Ag + ) by reducing to Ag 0 . These colloidal nanohybrids showed antibacterial activity against gram-negative and gram-positive bacterial strains, and the possible mechanism of killing bacterial cells could be membrane disruption. This synthetic strategy is facile and green, which helps avoid using toxic chemicals or reagents and complicated methods for colloidal nanohybrid preparation for biomedical applications. Supplementary Information The online version contains supplementary material available at 10.1038/s41598-024-78320-7.

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Peptide‐basedCoacervates: A Biomimetic Protocell

Cited by 2 publications

References 41 publications

Charge‐Mediated Interactions Affect Enzymatic Reactions in Peptide Condensates

Charge‐Mediated Interactions Affect Enzymatic Reactions in Peptide Condensates

Engineering of self-assembled silver-peptide colloidal nanohybrids with enhanced biocompatibility and antibacterial activity

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