Evidence map›Paper›PMID 36971982›Full record

ArticleProbiotics and antimicrobial proteins2024

Novel Antimicrobial Peptide SAAP Mutant as a Better Adjuvant to Sulbactam-Based Treatments Against Clinical Strains of XDR Acinetobacter baumannii.

Aniket Naha, Sudha Ramaiah

Abstract read
PubMed Publisher
In one paragraph

Article in Probiotics and antimicrobial proteins, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.2field-weighted citation impact, top 23% of its field
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

12 citing papers in PubMed, 13 citations in OpenAlex.

  1. Virulence · 2026
    Review
  2. Article
  3. Comparative genomics of carbapenem resistant and susceptible clinicalFrontiers in cellular and infection microbiology · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Review
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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 at 1 institution in 1 country.

Aniket NahaMedical and Biological Computing Laboratory, School of Bio-Sciences and Technology, Vellore Institute of Technology (VIT), Tamil Nadu, Vellore, 632014, India.ORCID 0000-0002-6811-9767
Sudha RamaiahMedical and Biological Computing Laboratory, School of Bio-Sciences and Technology, Vellore Institute of Technology (VIT), Tamil Nadu, Vellore, 632014, India. sudhaanand@vit.ac.in.ORCID 0000-0002-4800-329X
Vellore Institute of Technology University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The production of extended spectrum β-lactamases (ESBLs) in extensively drug-resistant (XDR) strains of Acinetobacter baumannii has created havoc amongst clinicians making the treatment procedure challenging. Carbapenem-resistant strains have displayed total ineffectiveness towards newer combinations of β-lactam-β-lactamase inhibitors (βL-βLI) in tertiary healthcare settings. Therefore, the present study was aimed to design potential β-lactamase antimicrobial peptide (AMP) inhibitors against ESBLs produced by the strains. We have constructed an AMP mutant library with higher antimicrobial efficacy (range: ~ 15 to 27%) than their parent peptides. The mutants were thoroughly screened based on different physicochemical and immunogenic properties revealing three peptides, namely SAAP-148, HFIAP-1, myticalin-C6 and their mutants with safe pharmacokinetics profile. Molecular docking highlighted SAAP-148_M15 displaying maximum inhibitory potential with lowest binding energies against NDM1 (- 1148.7 kcal/mol), followed by OXA23 (- 1032.5 kcal/mol) and OXA58 (- 925.3 kcal/mol). The intermolecular interaction profiles displayed SAAP-148_M15 exhibiting hydrogen bonds and van der Waals hydrophobic interactions with the crucial residues of metallo β-lactamase [IPR001279] and penicillin-binding transpeptidase [IPR001460] domains. Coarse-grained clustering and molecular dynamics simulations (MDS) further validated the stable backbone profile and minimal residue-level fluctuations of the protein-peptide complex that were maintained throughout the simulation timeframe. The present study hypothesised that the combination of sulbactam (βL) with SAAP-148_M15 (βLI) holds immense potential in inhibiting the ESBLs alongside restoration of sulbactam activity. The current in silico findings upon further experimental validations can pave path towards designing of successful therapeutic strategy against XDR strains of A. baumannii.

Indexed as

Acinetobacter baumanniiAcinetobacter InfectionsAnti-Bacterial AgentsAntimicrobial Peptidesbeta-Lactamase Inhibitorsbeta-LactamasesHumansMicrobial Sensitivity TestsMolecular Docking SimulationPenicillinsPeptidesSulbactamAnti-Bacterial AgentsAntimicrobial Peptidesbeta-Lactamase Inhibitorsbeta-LactamasesPenicillinsPeptidesSulbactamCoarse-grained clusteringImmunogenicityMolecular dockingMolecular dynamics simulationβ-lactamase

Identifiers

PMID36971982
OpenAlexW4360982788

What OpenQuestion holds

Textmetadata
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.