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Discovery of mammalian collagens I and III within ancient poriferan biopolymer spongin

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dc.abstract.enSpongin is a fundamental biopolymer that has played a crucial role in the skeletogenesis of keratosan sponges for over 800 million years. This biomaterial had so far remained chemically unidentified and believed to be an enigmatic type of halogenated collagen-keratin-based bioelastomer. Here we show collagen I and III as the main structural components of spongin. Proteomics, 13C solid state NMR and Raman spectroscopy confirm the identity of collagenous domains in spongin with collagen from mammals. Using an HPLC-MS analysis, we found halogenated di- and tri-tyrosines as crosslinking agents in spongin. Using molecular dynamics modeling, we solvated the crystal structures of collagen mimetic peptides for type I and type III collagens in four different systems, including selected brominated crosslinks. The results underscore the complex interplay between the collagen structures and crosslinks, raising intriguing questions about the molecular mechanisms underlying collagen chemistry within spongin as an ancient biocomposite.
dc.affiliationWydział Medycyny Weterynaryjnej i Nauk o Zwierzętach
dc.affiliation.instituteKatedra Fizjologii, Biochemii i Biostruktury Zwierząt
dc.contributor.authorEhrlich, Hermann
dc.contributor.authorMiksik, Ivan
dc.contributor.authorTsurkan, Mikhail V.
dc.contributor.authorSimon, Paul
dc.contributor.authorPorzucek, Filip
dc.contributor.authorRybka, Jakub Dalibor
dc.contributor.authorMankowska, Monika
dc.contributor.authorGalli, Roberta
dc.contributor.authorViehweger, Christine
dc.contributor.authorBrendler, Erica
dc.contributor.authorVoronkina, Alona
dc.contributor.authorPajewska-Szmyt, Martyna
dc.contributor.authorTabachnik, Aleksei
dc.contributor.authorTabachnick, Konstantin R.
dc.contributor.authorVogt, Carla
dc.contributor.authorWysokowski, Marcin
dc.contributor.authorJesionowski, Teofil
dc.contributor.authorBuchwald, Tomasz
dc.contributor.authorSzybowicz, Miroslaw
dc.contributor.authorSkieresz-Szewczyk, Kinga
dc.contributor.authorJackowiak, Hanna
dc.contributor.authorEreskovsky, Alexander
dc.contributor.authorde Alcântara, Amadeus C. S.
dc.contributor.authordos Santos, Alberto M.
dc.contributor.authorda Costa, Clauber H. S.
dc.contributor.authorArevalo, Sofia E.
dc.contributor.authorSkaf, Munir S.
dc.contributor.authorBuehler, Markus J.
dc.date.access2025-03-13
dc.date.accessioned2025-06-16T12:03:26Z
dc.date.available2025-06-16T12:03:26Z
dc.date.copyright2025-03-13
dc.date.issued2025
dc.description.abstract<jats:title>Abstract</jats:title> <jats:p>Spongin is a fundamental biopolymer that has played a crucial role in the skeletogenesis of keratosan sponges for over 800 million years. This biomaterial had so far remained chemically unidentified and believed to be an enigmatic type of halogenated collagen-keratin-based bioelastomer. Here we show collagen I and III as the main structural components of spongin. Proteomics, <jats:sup>13</jats:sup>C solid state NMR and Raman spectroscopy confirm the identity of collagenous domains in spongin with collagen from mammals. Using an HPLC-MS analysis, we found halogenated di- and tri-tyrosines as crosslinking agents in spongin. Using molecular dynamics modeling, we solvated the crystal structures of collagen mimetic peptides for type I and type III collagens in four different systems, including selected brominated crosslinks. The results underscore the complex interplay between the collagen structures and crosslinks, raising intriguing questions about the molecular mechanisms underlying collagen chemistry within spongin as an ancient biocomposite.</jats:p>
dc.description.accesstimeat_publication
dc.description.bibliographyil., bibliogr.
dc.description.financepublication_nocost
dc.description.financecost0,00
dc.description.if14,7
dc.description.points200
dc.description.versionfinal_published
dc.description.volume16
dc.identifier.doi10.1038/s41467-025-57460-y
dc.identifier.issn2041-1723
dc.identifier.urihttps://sciencerep.up.poznan.pl/handle/item/2856
dc.identifier.weblinkhttps://www.nature.com/articles/s41467-025-57460-y
dc.languageen
dc.pbn.affiliationbiological sciences
dc.relation.ispartofNature Communications
dc.relation.pagesart. 2515
dc.rightsCC-BY
dc.sciencecloudnosend
dc.share.typeOPEN_JOURNAL
dc.titleDiscovery of mammalian collagens I and III within ancient poriferan biopolymer spongin
dc.typeJournalArticle
dspace.entity.typePublication
oaire.citation.issue1
oaire.citation.volume16