ArticleRSC chemical biology2026
A truncated nisin variant, lipidated at its C-terminus, displays improved stability and increased antibacterial activity against methicillin-resistant
Article in RSC chemical biology, 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
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The rise of bacterial resistance has prompted researchers to shift their focus toward alternative antimicrobial agents, including antimicrobial peptides (AMPs). Some naturally occurring AMPs are lipidated, showing similarity with clinically used antimicrobial agents such as daptomycin and polymyxins, which are lipidated peptides. In this study, we investigate the impact of various lipid modifications on nisin. Nisin is a well-studied 34-amino acid AMP, ribosomally synthesized and post-translational modified, which is effective against many Gram-positive bacteria and is widely used as a food preservative. Wild-type nisin and two truncated forms, nisin(1-31) and nisin(1-20) were conjugated at the C-terminus with either a C4, C6, C8, or C10 lipid tail. Antimicrobial activity was assessed against two Gram-positive strains: methicillin-resistant
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.