{
  "id": 10458256,
  "title": "Native oligomerisation of a small type I antifreeze protein from winter flounder",
  "url": "https://urgent.news/2026/09/28/native-oligomerisation-of-a-small-type-i-antifreeze-protein-from",
  "topic": "science",
  "section": "Science",
  "published": "2026-09-28T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.09.25.754443v1?rss=1"
  },
  "original_language": "en",
  "account": "Antifreeze proteins and peptides work by attaching to ice crystals and preventing their growth, leading to a decrease in the freezing point. AFP6, a common antifreeze peptide in winter flounder blood serum, is made up of 37 amino acids and has a helical structure with a hydrophobic side that interacts with ice. In this investigation, researchers used computer simulations to model the peptide and discovered that it could form an antiparallel dimer, with the hydrophobic faces of the helices buried within the structure. The study examined the oligomerization of both non-amidated and synthetic amidated forms of AFP6 in water using several techniques. Crosslinking of the non-amidated AFP6 and subsequent electrophoresis revealed that the peptide formed dimers, while the amidated form and a mutant also indicated the presence of trimers and tetramers. Crosslinking of the non-amidated AFP6 under different conditions showed that monomers and dimers were predominant, with smaller amounts of tetrameric oligomers. However, only monomers and dimers were observed in AFP6 treated with sodium bicarbonate. The isolated oligomers produced ice crystal formations and thermal hysteresis similar to the original peptide, suggesting that oligomerization did not hinder the peptide's interaction with ice. Instead, oligomerization might improve the peptide's solubility in water, as this is the first AFP oligomer to show no impact on ice interaction.",
  "summary": "Antifreeze proteins and peptides adhere to the surfaces of ice crystals and inhibit their growth, resulting in non-colligative freezing point depression. AFP6 is a predominant antifreeze peptide in the blood serum of winter flounder (Pseudopleuronectes americanus). This 37-residue amphiphilic -helical peptide can be dissolved in water; however, its ice-binding surface is the hydrophobic side of…",
  "key_points": [],
  "editors_take": null,
  "illustration": null,
  "coverage": {
    "outlets": 1,
    "also_reported_by": []
  },
  "ai_generated": true,
  "disclaimer": "Summaries, key points and the editor’s take are written by software from other outlets’ reporting and may contain errors — always check the linked original."
}