{
  "abstract": "Branched antimicrobial peptides offer a promising strategy for improving the stability and activity of membrane-active peptides, but how branching alters self-association and membrane binding remains unclear. We used all-atom molecular dynamics simulations to compare tetra-branched SET-M33 with its linear branch sequence Q33 (KKIRVRLSA) in water and at an anionic bacterial-membrane model, to do this, systems containing equivalent numbers of Q33 sequence units were simulated. Q33 formed dimers and higher-order oligomers, particularly at the membrane interface and under hydration-tuned enhanced sampling. In contrast, SET-M33 remained more dispersed, as the branched scaffold and its high cationic charge limited peptide-peptide association while allowing multivalent membrane binding. Both architectures associated rapidly with the bilayer but remained predominantly surface-bound, without persistent pore formation or complete insertion. Q33 showed stronger membrane-induced helical stabilization, whereas SET-M33 retained a more heterogeneous conformational ensemble. Overall, branching primarily altered lateral peptide organization while preserving close membrane association, suppressing uncontrolled self-aggregation and providing an atomistic rationale for the distinct behavior of SET-M33 relative to Q33.",
  "abstract_shown": true,
  "affiliations": [
    "Istituto Italiano di Tecnologia"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 6,
  "authors": [
    {
      "name": "S. Satvati"
    },
    {
      "name": "M. Rigoli"
    },
    {
      "name": "S. Fortuna"
    },
    {
      "name": "C. Falciani"
    },
    {
      "name": "A. Pini"
    },
    {
      "affs": [
        0
      ],
      "name": "W. Rocchia"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/c1x8s8yzgm3et.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.10.12.757849",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.10.12.757849v1.full",
  "id": "c1x8s8yzgm3et",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.10.12.757849v1",
  "language": null,
  "licence": "CC-BY-NC-ND",
  "licence_label": "CC BY-NC-ND",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "biophysics"
    ],
    [
      "openalex",
      "2404|Antimicrobial Peptides and Activities"
    ]
  ],
  "openalex": "W7221669807",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.10.12.757849v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-12",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/c1x8s8yzgm3et.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:27:38Z",
      "native_id": "10.64898/2026.10.12.757849",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.10.12.757849v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "biorxiv:biophysics",
      "subfield": "biophysics"
    }
  ],
  "title": "Branching Suppresses Self-Aggregation while Preserving Membrane Association in SET-M33: An Atomistic Molecular Dynamics Study",
  "title_text": "Branching Suppresses Self-Aggregation while Preserving Membrane Association in SET-M33: An Atomistic Molecular Dynamics Study",
  "type": "preprint",
  "updated_at": "2026-10-30T12:27:38Z",
  "url": "https://research.draconitic.com/paper/c1x8s8yzgm3et",
  "venue": "bioRxiv",
  "versions": []
}