ArticleBrazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]2026
From decay to discovery: A new antimicrobial peptide from Chrysomya megacephala (Diptera: Calliphoridae) larvae.
Article in Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 2026. 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
The larvae of Chrysomya megacephala (Diptera: Calliphoridae) thrive in environments rich in decaying organic matter and dead animals, which are often colonized by bacteria. This adaptation suggests the larvae possess antimicrobial substances that provide them with a defense against bacterial infection. The hemolymph from around 200 C. megacephala larvae previously exposed to methicillin-resistant Staphylococcus aureus (MRSA) (clinical isolate) was collected, purified, and isolated utilizing Reverse Phase High Performance Liquid Chromatography (RP-HPLC). Fractions exhibiting antimicrobial properties underwent further analysis using Quadrupole Time-of-Flight Liquid Chromatography Mass Spectrometry (QTOF-LCMS). The resulting mass spectra were translated into amino acid sequences through de novo algorithms. Antimicrobial prediction tools from repositories such as APD3, Database of Antimicrobial Activity and Structure of Peptides (DBSAAP), Database of Antimicrobial Peptide (DBAMP), and Collection of Antimicrobial Peptide Version 4 (CAMPR4) were employed to validate the peptide sequences. We found the peptide (HGCGRLSKWFRQPGLLLSVKR) exhibited partial similarity with C. megacephala's heat shock protein 70 (hsp70). The peptide demonstrated activity against Staphylococcus aureus, including MRSA, Micrococcus luteus, Staphylococcus epidermidis, and Bacillus subtilis with a minimum inhibitory concentration (MIC) of 0.06 mg/ml and an inhibition zone ranging from 8 to 11 mm at a concentration of 1 mg/ml. The cytotoxicity test of the peptide on immortalized keratinocyte cells (HaCat) and human corneal epithelial cells (HCEC) revealed an average cell viability > 80% at concentration of 0.06 mg/ml. In conclusion, the novel peptide (HGCGRLSKWFRQPGLLLSVKR) exhibits a broad spectrum of activity against Gram-positive bacteria while demonstrating minimal toxicity towards human cells.
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.