Evidence map›Paper›PMID 39998115›Full record

ArticleToxins2025

Synthesis and Evaluation of Melittin-Modified Peptides for Antibacterial Activity.

Xiangxiang Xu, Hongyi Fu, Weihui Wu, Liang Zong, Dan Li, Bo Zhuang, Yelin Qi, Xiuli Qi, Ting Liang

Abstract read
In one paragraph

Article in Toxins, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Therapeutic Bioactivity Exerted by theMolecules (Basel, Switzerland) · 2025
    Article
  3. Research Progress in Medical Biomaterials for Bone Infections.Journal of functional biomaterials · 2025
    Review
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

9 authors.

Xiangxiang XuInstitute of NBC Deffence, Beijing 102205, China.
Hongyi FuInstitute of NBC Deffence, Beijing 102205, China.
Weihui WuInstitute of NBC Deffence, Beijing 102205, China.
Liang ZongInstitute of NBC Deffence, Beijing 102205, China.
Dan LiInstitute of NBC Deffence, Beijing 102205, China.
Bo ZhuangInstitute of NBC Deffence, Beijing 102205, China.
Yelin QiInstitute of NBC Deffence, Beijing 102205, China.
Xiuli QiInstitute of NBC Deffence, Beijing 102205, China.
Ting LiangInstitute of NBC Deffence, Beijing 102205, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Melittin, a naturally occurring antimicrobial peptide, demonstrates broad-spectrum activity, effectively suppressing and eliminating both Gram-positive and Gram-negative bacteria, including specific drug-resistant strains. In this study, molecular simulation software was employed to investigate and modify the structure of melittin with the aim of synthesizing a modified peptide exhibiting enhanced antibacterial potency and assessing its bacteriostatic and antibacterial properties. The primary research objectives were as follows: 1. Preparation and characterization of melittin-modified peptide-Using molecular simulation software, the structure of the melittin-modified peptide was adjusted to predict its activity and select the most appropriate amino acid sequence. The peptide was synthesized through solid-phase peptide synthesis employing the Fmoc strategy and subsequently purified using liquid chromatography. The yield of the purified modified melittin was determined to be 30.97%, and the identity of the product was confirmed by LC-MS and MALDI-TOF-MS. 2. Evaluation of the antimicrobial activity of the melittin-modified peptide-The minimum inhibitory concentration (MIC) and minimum bactericidal concentration (MBC) of melittin and its modified peptide were measured using gradient dilution and plate counting techniques. The results revealed that both melittin and its modified peptide exhibited strong antibacterial efficacy against Gram-positive and Gram-negative bacteria, as well as certain drug-resistant strains. This showed that melittin and its modified peptide have the same antibacterial (killing) effect. A scanning electron microscope analysis indicated that both melittin and its modified peptide were capable of disrupting bacterial cell structures, leading to bacterial cell death.

Indexed as

Anti-Bacterial AgentsMelittenAmino Acid SequenceAntimicrobial PeptidesGram-Negative BacteriaGram-Positive BacteriaMicrobial Sensitivity TestsAnti-Bacterial AgentsAntimicrobial PeptidesMelittenantimicrobial propertymelittin-modified peptidesolid-phase synthesis

Identifiers

PMID39998115
PMCPMC11860715

What OpenQuestion holds

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Registered trials

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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.