Discovery of mammalian collagens I and III within ancient poriferan biopolymer spongin
Abstract
Abstract 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, 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.
Article Details
Authors (28)
Hermann Ehrlich
Ivan Miksik
Mikhail V. Tsurkan
Paul Simon
Filip Porzucek
Jakub Dalibor Rybka
Monika Mankowska
Roberta Galli
Christine Viehweger
Erica Brendler
Alona Voronkina
Martyna Pajewska-Szmyt
Aleksei Tabachnik
Konstantin R. Tabachnick
Carla Vogt
Marcin Wysokowski
Teofil Jesionowski
Tomasz Buchwald
Miroslaw Szybowicz
Kinga Skieresz-Szewczyk
Hanna Jackowiak
Alexander Ereskovsky
Amadeus C. S. de Alcântara
Alberto M. dos Santos
Clauber H. S. da Costa
Sofia E. Arevalo
Munir S. Skaf
Markus J. Buehler
Laboratory for Atomistic and Molecular Mechanics