ArticleScientific reports2025
Discovery of hyde C1 a broad spectrum antimicrobial peptide derived from chicory.
Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Antimicrobial peptides (AMPs) are emerging as promising alternatives to traditional antibiotics against multidrug-resistant (MDR) bacteria. In this study, we isolated and characterized a novel AMP, named Hyde C1, from the chicory plant (Cichorium intybus L.). Hyde C1 was purified using reverse-phase high-performance liquid chromatography (RP-HPLC) and determined to have a molecular weight of 3686.4 Da. It exhibits strong antibacterial activity against both Gram-positive (S. aureus ATCC 29213) and Gram-negative (E. coli ATCC 25922, P. aeruginosa ATCC 27853, A. baumannii ATCC 19606) bacteria, with minimum inhibitory concentrations (MICs) ranging from 2 to 16 µg/mL. Hyde C1 disrupts bacterial membranes, as evidenced by increased permeability, membrane depolarization, and scanning electron microscopy. Bioinformatic analysis revealed its amphipathic α-helical structure, with a high hydrophobic ratio (61%) and a net positive charge (+ 6), supporting its bactericidal mechanism. The peptide also demonstrated high stability under various pH, temperature, and salt conditions, along with low hemolytic and cytotoxic effects. These properties suggest that Hyde C1 is a strong candidate for development as a novel antimicrobial agent.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.