Evidence map›Paper›PMID 40911851›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2025

Myelin-Proteinoids Interactions in Neural Signaling.

Panagiotis Mougkogiannis, Andrew Adamatzky

Abstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Proteinoid Computing on Olivine Substrates.Langmuir : the ACS journal of surfaces and colloids · 2026
    Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Panagiotis MougkogiannisUnconventional Computing Laboratory, University of the West of England, Bristol BS16 1QY, U.K.ORCID 0000-0003-1710-4917
Andrew AdamatzkyUnconventional Computing Laboratory, University of the West of England, Bristol BS16 1QY, U.K.ORCID 0000-0003-1073-2662

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study examines how proteinoids and myelin interact in biomimetic neural systems. These interactions reveal electrochemical properties and computing capabilities. Proteinoids are made when amino acids heat up and bond together. They form microspheres that can produce electrical signals on their own. Myelin, on the other hand, acts as an insulator and conductor, which is essential for nerve signaling. We studied proteinoid-myelin hybrid systems. We used scanning electron microscopy, electrochemical impedance spectroscopy, and recorded extracellular potential for over 180,000 s. The hybrid structures show complex electrical behaviors. These include spontaneous spike generation, phase transitions, and oscillatory patterns. The membrane potentials range from -90 mV to +70 mV. Equivalent circuit analysis showed that hybrid systems had higher capacitance (159.3 nF) and lower impedance (3.934 kΩ) than pure proteinoid microspheres. We used threshold-based signal processing to perform full Boolean logic operations. This was done by tapping into the bioelectrical activity of these hybrid systems. This research shows that simple biomolecular parts can come together to form structures. These structures can perform complex computations. This finding hints at uses in biocompatible computing, neuromorphic engineering, and bioelectronic interfaces.

Indexed as

Myelin SheathAnimalsSignal Transduction

Identifiers

PMID40911851
PMCPMC12444999

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.