Spongin

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Spongin, a modified type of collagen protein, forms the fibrous skeleton of most organisms among the phylum Porifera, the sponges. It is secreted by sponge cells known as spongocytes. [1]

Contents

Spongin gives a sponge its flexibility. True spongin is found only in members of the class Demospongiae. [2] Its molecular structure remains incompletely characterized, however it shares similarities with both collagen and keratin. [3] [4] [5]

Research directions

Use in the removal of phenolic compounds from wastewater

Researchers have found spongin to be useful in the photocatalytic degradation and removal of bisphenols (such as BPA) in wastewater. A heterogeneous catalyst consisting of a spongin scaffold for iron phthalocyanine (SFe) in conjunction with peroxide and UV radiation has been shown to remove phenolic wastes more quickly and efficiently than conventional methods. [6] Other research using spongin scaffolds for the immobilization of Trametes versicolor Laccase has shown similar results in phenol degradation. [7]

Molecular structure

Structure of spongin remains incompletely understood due to limitations in protein analytical methods. Although its chemical composition shares some features with collagen and keratin, spongin is a distinct biopolymer characterized by halogenated amino acids, primary bromine, with smaller amounts of iodine and chlorine. Additionally, the presence of xylose and significant mineralization with calcium carbonates and silica further differentiates spongin from collagen and keratin. [8] [9]

Collagen-like characteristics

Spongin and collagen exhibit comparable filament structure, both displaying a hierarchical organization of nanofibrils, microfibrils, and fibers, as well as a triple-helical based structure. Spongin microfibrilis measure approximately 10nm in diameter and exhibit a periodic banding pattern every 60nm, comparing to collagen's 67nm periodicity. [10] Despite the structural similarities, amino acid analysis reveals that spongin contains significantly higher levels of tyrosine residues, approximately 90% of which are mono- or di-brominated derivatives. This abundance of tyrosine is related to the oxidation of phenylalanine residues, which are prevalent in collagen but nearly absent in spongin. The brominated tyrosine derivatives are hypothesized to play a crucial role in stabilizing spongin's triple-helical structure through cross-linking. [9]

Keratin-like characteristics

Spongin also exhibits compositional similarities to keratin, particularly in its sulfur content and thermal stability. It withstands temperatures up to 300ºC, which is more characteristic for keratin than collagen. However, due to spongin's distinct biochemical features, its full molecular classification remains unknown. [8]

References

  1. ↑ Anderson, D. (2001). Invertebrate Zoology. Oxford University Press.
  2. ↑ Brusca, R.; Brusca, G. (2003). Invertebrate Zoology. Sinauer Associates. p. 191.
  3. ↑ Kubiak, Anita; Pajewska-Szmyt, Martyna; Kotula, Martyna; Leśniewski, Bartosz; Voronkina, Alona; Rahimi, Parvaneh; Falahi, Sedigheh; Heimler, Korbinian; Rogoll, Anika; Vogt, Carla; Ereskovsky, Alexander; Simon, Paul; Langer, Enrico; Springer, Armin; Förste, Maik (2023-08-22). "Spongin as a Unique 3D Template for the Development of Functional Iron-Based Composites Using Biomimetic Approach In Vitro". Marine Drugs. 21 (9): 460. doi: 10.3390/md21090460 . ISSN   1660-3397. PMC   10532518 . PMID   37755073.
  4. ↑ Ehrlich, Hermann; Miksik, Ivan; Tsurkan, Mikhail V.; Simon, Paul; Porzucek, Filip; Rybka, Jakub Dalibor; Mankowska, Monika; Galli, Roberta; Viehweger, Christine; Brendler, Erica; Voronkina, Alona; Pajewska-Szmyt, Martyna; Tabachnik, Aleksei; Tabachnick, Konstantin R.; Vogt, Carla (2025-03-13). "Discovery of mammalian collagens I and III within ancient poriferan biopolymer spongin". Nature Communications. 16 (1): 2515. Bibcode:2025NatCo..16.2515E. doi:10.1038/s41467-025-57460-y. ISSN   2041-1723. PMC   11906918 . PMID   40082406.
  5. ↑ Szatkowski, Tomasz; Jesionowski, Teofil (2017), Ehrlich, Hermann (ed.), "Hydrothermal Synthesis of Spongin-Based Materials", Extreme Biomimetics, Cham: Springer International Publishing, pp. 251–274, Bibcode:2017exbi.book..251S, doi:10.1007/978-3-319-45340-8_10, ISBN   978-3-319-45340-8 , retrieved 2025-05-03
  6. ↑ Norman, Żółtowska-Aksamitowska, Zgoła-Grześkowiak, Ehrlich, and Jesionowski. "Iron(III) Phthalocyanine Supported on a Spongin Scaffold as an Advanced Photocatalyst in a Highly Efficient Removal Process of Halophenols and Bisphenol A." Journal of Hazardous Materials 347 (2018): 78-88. Web.
  7. ↑ Zdarta, Antecka, Frankowski, Zgoła-Grześkowiak, Ehrlich, and Jesionowski. "The Effect of Operational Parameters on the Biodegradation of Bisphenols by Trametes Versicolor Laccase Immobilized on Hippospongia Communis Spongin Scaffolds." Science of the Total Environment 615 (2018): 784-95. Web.
  8. 1 2 Kubiak, Anita; Pajewska-Szmyt, Martyna; Kotula, Martyna; Leśniewski, Bartosz; Voronkina, Alona; Rahimi, Parvaneh; Falahi, Sedigheh; Heimler, Korbinian; Rogoll, Anika; Vogt, Carla; Ereskovsky, Alexander; Simon, Paul; Langer, Enrico; Springer, Armin; Förste, Maik (2023-08-22). "Spongin as a Unique 3D Template for the Development of Functional Iron-Based Composites Using Biomimetic Approach In Vitro". Marine Drugs. 21 (9): 460. doi: 10.3390/md21090460 . ISSN   1660-3397. PMC   10532518 . PMID   37755073.
  9. 1 2 Ehrlich, Hermann; Miksik, Ivan; Tsurkan, Mikhail V.; Simon, Paul; Porzucek, Filip; Rybka, Jakub Dalibor; Mankowska, Monika; Galli, Roberta; Viehweger, Christine; Brendler, Erica; Voronkina, Alona; Pajewska-Szmyt, Martyna; Tabachnik, Aleksei; Tabachnick, Konstantin R.; Vogt, Carla (2025-03-13). "Discovery of mammalian collagens I and III within ancient poriferan biopolymer spongin". Nature Communications. 16 (1): 2515. Bibcode:2025NatCo..16.2515E. doi:10.1038/s41467-025-57460-y. ISSN   2041-1723. PMC   11906918 . PMID   40082406.
  10. ↑ Szatkowski, Tomasz; Jesionowski, Teofil (2017), Ehrlich, Hermann (ed.), "Hydrothermal Synthesis of Spongin-Based Materials", Extreme Biomimetics, Cham: Springer International Publishing, pp. 251–274, Bibcode:2017exbi.book..251S, doi:10.1007/978-3-319-45340-8_10, ISBN   978-3-319-45340-8 , retrieved 2025-05-03


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