Minimal structural changes alter membrane interaction of short antimicrobial peptides: experimenta

Study citation and publication details

The PubMed record documents an article in European Journal of Medicinal Chemistry: “Effect of minimal structural modifications on the membrane interaction of short antimicrobial peptides: An experimental and computational study.” The entry lists PMID 42030711 and DOI 10.1016/j.ejmech.2026.118859. The article is shown as Epub April 15, 2026, with the journal issue reference 2026 Aug 5:312:118859.

The PubMed page includes the publisher link (Elsevier Science) among the full-text links. The record shows standard PubMed navigation elements and options (save, email, collections) and reports that full-text options can be retrieved via the publisher link provided on the PubMed entry.

Authors and institutional affiliations

The author list on the PubMed entry begins with Lucia Ferrazzano and includes Francesca Bonvicini, Saha Satvati, Dario Corbisiero, Silvia Rizzo, Ilaria Di Stefano, Paolo Cantelmi, Silvia Panzavolta, Giovanna A Gentilomi, Walter Rocchia, Walter Cabri, and Alessandra Tolomelli. Affiliations are provided and show multi-institutional collaboration across Italian research centers, including:

• P4i Lab - Peptidomimetics and Peptides Targeting Protein-Protein Interaction, Department of Chemistry "Giacomo Ciamician", Alma Mater Studiorum - University of Bologna.
• Department of Pharmacy and Biotechnology, Alma Mater Studiorum - University of Bologna.
• CONCEPT Lab, Fondazione Istituto Italiano di Tecnologia (IIT), Genova; Department of Biotechnology, Chemistry and Pharmacy, University of Siena; and SetLance srl, Siena.
• Biological Structures and Materials Lab, Department of Chemistry "Giacomo Ciamician", University of Bologna.
• Division of Microbiology, IRCCS Azienda Ospedaliero-Universitaria di Bologna.

Corresponding electronic addresses are reported for at least two authors in the PubMed record.

Scope and research approach indicated by the title

The article’s title indicates the study focused on how minimal structural modifications influence the membrane interaction of short antimicrobial peptides, employing both experimental and computational methodologies.

From the title alone, the intended scope is to probe structure–activity or structure–interaction relationships at a fine scale — specifically, to evaluate whether small alterations in peptide structure change the way short antimicrobial peptides interact with membranes. The combination of experimental and computational methods implied by the title suggests the authors integrated laboratory assays with in silico modelling or simulations to characterize peptide–membrane interactions.

Available record elements on PubMed

The supplied PubMed content includes:

• Full bibliographic citation (journal, authors, DOI, PMID, Epub date).
• Author names and detailed affiliations.
• A link to Elsevier Science for full-text access.

The PubMed page also shows the usual site navigation and account features; however, the supplied content does not include the article abstract text, figures, tables, experimental details, or study conclusions.

Missing information and limitations of the supplied source

The PubMed content provided here does not contain key elements needed to summarize the study’s findings or methods. Specifically, the following were not reported in the supplied source text:

• The peptide sequences or chemical structures studied.
• The precise nature of the “minimal structural modifications” examined (for example, residue substitutions, terminal modifications, cyclization, or backbone changes).
• The experimental assays used to measure membrane interaction (e.g., liposome leakage, circular dichroism, fluorescence spectroscopy, microscopy) and their results.
• Computational methods and parameters (e.g., molecular dynamics simulations, force fields, membrane models, simulation times) and outcomes.
• Quantitative results, statistical analyses, or authors’ conclusions regarding how specific modifications affected membrane interaction or antimicrobial activity.
• Any reported implications for antimicrobial development, toxicity, or translational potential.

Because these core details are absent from the supplied record, this rewritten summary refrains from inferring results or conclusions that are not explicitly present in the provided PubMed content.

How to access full text and next steps for readers

The PubMed entry includes a link to Elsevier Science for full-text retrieval. Readers seeking the study’s methods, data, and conclusions should consult the publisher’s full text or the complete PubMed abstract (if available on the live PubMed page). The DOI (10.1016/j.ejmech.2026.118859) and PMID (42030711) are provided in the record and can be used to locate the full article through institutional access, interlibrary loan, or the publisher’s site.

Notes and limitations: the information in this summary is limited to bibliographic and page-level data present on the supplied PubMed record. No experimental details, computational results, or author conclusions were included in the supplied source text; therefore, this document does not report any study-specific outcomes or recommendations.