Ambiguity between Adaptation and Aggregation of Intrinsically Disordered Fish Proteins: Antifreeze-like or Amyloid-like?

Ambiguity between Adaptation and Aggregation of Intrinsically Disordered Fish Proteins: Antifreeze-like or Amyloid-like? | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Article Ambiguity between Adaptation and Aggregation of Intrinsically Disordered Fish Proteins: Antifreeze-like or Amyloid-like? Anusmita Hait, Seetharaman Balaji This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-8284559/v1 This work is licensed under a CC BY 4.0 License Status: Posted Version 1 posted You are reading this latest preprint version Abstract Antifreeze proteins (AFPs) play a crucial role in the survival of fish species by inhibiting ice crystal growth. In this study, a comprehensive in silico characterization of an uncharacterized AFP sequence from Arctogadus glacialis along with other fishes was performed. Sequence analysis revealed the presence of extensive tandem repeats, suggesting a modular architecture typical of AFPs. The predicted molecular weight of the protein was 185.1 kDa, with a theoretical isoelectric point ranging between 5.54 and 5.73 and a net charge of − 16.5 at pH 7.0. Amino acid composition analysis indicated threonine (8.6%) and leucine (8.2%) as the most abundant residues, while tryptophan (0.9%) and lysine (1.2%) were least represented. The protein exhibited an aliphatic index of 75.79, a GRAVY value of − 0.147, and an instability index of 52.13, suggesting moderate thermostability and hydrophilicity. Secondary structure prediction indicated a predominance of random coils (53.65%) in the protein; comparative analysis showed a higher random coil (57.54%) structure in lamprey AFPs. Tertiary structure modeling yielded a pTM score of 0.43, supporting a partially ordered structure with flexible loop regions. Conserved domain analysis identified a key motif spanning residues 1471–1520, potentially involved in ice-binding. Phylogenetic analysis of AFPs from host and parasitic fish species revealed evolutionary clustering consistent with adaptation to unfamiliar environments. Collectively, these findings provide the first computational insights into the structural and functional features of A. glacialis AFP, contributing to the broader understanding of antifreeze mechanisms among fishes. Biological sciences/Biochemistry Biological sciences/Computational biology and bioinformatics Biological sciences/Evolution Biological sciences/Structural biology Antifreeze proteins Arctogadus glacialis Lamprey Amyloid Adaptation Full Text Additional Declarations No competing interests reported. Cite Share Download PDF Status: Posted Version 1 posted You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. We do this by developing innovative software and high quality services for the global research community. Our growing team is made up of researchers and industry professionals working together to solve the most critical problems facing scientific publishing. Also discoverable on Platform About Our Team In Review Editorial Policies Advisory Board Help Center Resources Author Services Accessibility API Access RSS feed Manage Cookie Preferences © Research Square 2026 | ISSN 2693-5015 (online) Privacy Policy Terms of Service Do Not Sell My Personal Information {"props":{"pageProps":{"initialData":{"identity":"rs-8284559","acceptedTermsAndConditions":true,"allowDirectSubmit":true,"archivedVersions":[],"articleType":"Article","associatedPublications":[],"authors":[{"id":570212039,"identity":"78210e22-c725-4c99-8aa0-f2fe51a18fe4","order_by":0,"name":"Anusmita Hait","email":"","orcid":"","institution":"Manipal Academy of Higher Education","correspondingAuthor":false,"prefix":"","firstName":"Anusmita","middleName":"","lastName":"Hait","suffix":""},{"id":570212040,"identity":"1c7e086c-b896-4244-a0bf-47c3cf711181","order_by":1,"name":"Seetharaman 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