Thermosensory spiking activity of proteinoid microspheres cross-linked by actin filaments

Mougkogiannis, Panagiotis; Adamatzky, Andrew

Abstract

Actin, found in all eukaryotic cells as globular (G) or filamentous (F) actin, undergoes polymerization, with G-actin units changing shape to become F-actin. Thermal proteins, or proteinoids, are created by heating amino acids (160-200 °C), forming polymeric chains. These proteinoids can swell in an aqueous solution at around 50 °C, producing hollow microspheres filled with a solution, exhibiting voltage spikes. Our research explores the signaling properties of proteinoids, actin filaments, and hybrid networks combining actin and proteinoids. Proteinoids replicate brain excitation dynamics despite lacking specific membranes or ion channels. We investigate enhancing conductivity and spiking by using pure actin, yielding improved coordination in networks compared with individual filaments or proteinoids. Temperature changes (20 short-peptide supramolecular C to 80 °C) regulate conduction states, demonstrating external control over emergent excitability in protobrain systems. Adding actin to proteinoids reduces spike timing variability, providing a more uniform feature distribution. These findings support theoretical models proposing cytoskeletal matrices for functional specification in synthetic protocell brains, promoting stable interaction complexity. The study concludes that life-like signal encoding can emerge spontaneously within biological polymer scaffolds, incorporating abiotic chemistry.

Citation

Mougkogiannis, P., & Adamatzky, A. (2024). Thermosensory spiking activity of proteinoid microspheres cross-linked by actin filaments. Langmuir, 40, 12649–12670. https://doi.org/10.1021/acs.langmuir.4c01107

• Journal Article Type: Article
• Acceptance Date: May 27, 2024
• Online Publication Date: Jun 5, 2024
• Publication Date: Jun 18, 2024
• Deposit Date: Jun 5, 2024
• Publicly Available Date: Jun 18, 2024
• Journal: Langmuir
• Print ISSN: 0743-7463
• Electronic ISSN: 1520-5827
• Publisher: American Chemical Society
• Peer Reviewed: Peer Reviewed
• Volume: 40
• Pages: 12649–12670
• DOI: https://doi.org/10.1021/acs.langmuir.4c01107
• Public URL: https://uwe-repository.worktribe.com/output/12035558