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Comparative mucomic analysis of three functionally distinct Cornu aspersum Secretions
Open accessAbstract
Every animal secretes mucus, placing them among the most diverse biological materials. Mucus hydrogels are complex mixtures of water, ions, carbohydrates, and proteins. Uncertainty surrounding their composition and how interactions between components contribute to mucus function complicates efforts to exploit their properties. There is substantial interest in commercializing mucus from the garden snail, Cornu aspersum , for skincare, drug delivery, tissue engineering, and composite materials. C. aspersum secretes three mucus—one shielding the animal from environmental threats, one adhesive mucus from the pedal surface of the foot, and another pedal mucus that is lubricating. It remains a mystery how compositional differences account for their substantially different properties. Here, we characterize mucus proteins, glycosylation, ion content, and mechanical properties that could be used to provide insight into structure-function relationships through an integrative “mucomics” approach. We identify macromolecular components of these hydrogels, including a previously unreported protein class termed Conserved Anterior Mollusk Proteins (CAMPs). Revealing differences between C. aspersum mucus shows how considering structure at all levels can inform the design of mucus-inspired materials.
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Peptides in C. aspersum mucous secretions are characterized by excessive amounts of Ser/Thr residues, N-acetylgalactosamine, galactose, and fucose glycans; their average molecular weight is 30 kDa, unlike mammalian mucins, which usually have a larger mass ranging from 100 kDa to 1 MDa with a large amount of sialic acids.
“Peptides in C. aspersum mucous secretions are characterized by excessive amounts of Ser/Thr residues, N-acetylgalactosamine, galactose, and fucose glycans. Their average molecular weight is 30 kDa, unlike mammalian mucins, which usually have a larger mass ranging from 100 kDa to 1 MDa with a large amount of sialic acids.”
From Chemical Variability and Biological Potential of Cornu aspersum Mucus as a Source for the Development of New Cosmetic and Pharmaceutical Products (2025) · cites this paper as [31]
Mollusk mucus contains proteins and glycans that are not found in mammalian mucus.
“In addition, mollusk mucus contains proteins and glycans that are not found in mammalian mucus [31].”
From Chemical Variability and Biological Potential of Cornu aspersum Mucus as a Source for the Development of New Cosmetic and Pharmaceutical Products (2025) · cites this paper as [31]
The protein concentration in the resuspended crude C. aspersum mucus solution reached about 77-170 g/L.
“According to Cerullo et al. (2023), the protein concentration in the resuspended crude mucus solution reached about 77–170 g/L [31].”
From Chemical Variability and Biological Potential of Cornu aspersum Mucus as a Source for the Development of New Cosmetic and Pharmaceutical Products (2025) · cites this paper as [31]
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Citations
Cites
Potter, S. C., Luciani, A., Eddy, S. R., Park, Y., Lopez, R., & Finn, R. D. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky448 · Cited by 2,607
Biological hydrogels as selective diffusion barriers
Lieleg, O., & Ribbeck, K. (2011) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.06.002 · Cited by 387
Tenascin-X: beyond the architectural function
Valcourt, U., Alcaraz, L. B., Exposito, J.-Y., Lethias, C., & Bartholin, L. (2015) · Cell Adhesion & Migration · doi:10.4161/19336918.2014.994893 · Cited by 132
Advancing Discovery of Snail Mucins Function and Application
McDermott, M., Cerullo, A. R., Parziale, J., Achrak, E., Sultana, S., Ferd, J., Samad, S., Deng, W., Braunschweig, A. B., & Holford, M. (2021) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2021.734023 · Cited by 77
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Research works printed but not linked: 102
- Cerullo, A. R. et al. Comparative animal mucomics: Inspiration for functional materials from ubiquitous and understudied biopolymers. ACS Biomater. Sci. Eng. 6, 5377–5398 (2020). · DOI
- Zhong, T., Min, L., Wang, Z., Zhang, F. & Zuo, B. Controlled self-assembly of glycoprotein complex in snail mucus from lubricating liquid to elastic fiber. RSC Adv. 8, 13806–13812 (2018). · DOI
- Co, J. Y., Crouzier, T. & Ribbeck, K. Probing the role of mucin-bound glycans in bacterial repulsion by mucin coatings. Adv. Mater. Interfaces 2, 1500179 (2015). · DOI
- Allam, B. & Espinosa, E. P. in Mucosal Health in Aquaculture 325–370 (Elsevier, 2015). · DOI
- McShane, A. et al. Mucus. Curr. Biol. 31, R938–R945 (2021). · DOI
- Denny, M. Locomotion: the cost of gastropod crawling. Science 208, 1288–1290 (1980). · DOI
- Hughes, G. W. et al. The MUC5B mucin polymer is dominated by repeating structural motifs and its topology is regulated by calcium and pH. Sci. Rep. 9, 1–13 (2019). · DOI
- Witten, J., Samad, T. & Ribbeck, K. Molecular characterization of mucus binding. Biomacromolecules 20, 1505–1513 (2019). · DOI
- Gabriel, U. I., Mirela, S. & Ionel, J. Quantification of mucoproteins (glycoproteins) from snails mucus, Helix aspersa and Helix Pomatia. J. Agroalimentary Process. Technol. 17, 410–413 (2011).
- Kimura, K., Chiba, S. & Koene, J. M. Common effect of the mucus transferred during mating in two dart-shooting snail species from different families. J. Exp. Biol. 217, 1150–1153 (2014). · DOI
- Dolashki, A. et al. Structure and antibacterial activity of isolated peptides from the mucus of garden snail Cornu aspersum. Bulg. Chem. Commun. 50, 195–200 (2018).
- Vong, A., Ansart, A. & Dahirel, M. Dispersers are more likely to follow mucus trails in the land snail Cornu aspersum. Sci. Nat. 106, 43 (2019). · DOI
- Allam, B. & Espinosa, E. P. in Mucosal Health in Aquaculture (eds Beck, B. H. & Peatman, E.) 325–370 (Academic Press, 2015). · DOI
- Pruitt, K. D., Tatusova, T. & Maglott, D. R. NCBI Reference Sequence (RefSeq): a curated non-redundant sequence database of genomes, transcripts and proteins. Nucleic Acids Res. 33, D501–D504 (2005). · DOI
- Ballance, S. et al. Partial characterisation of high-molecular weight glycoconjugates in the trail mucus of the freshwater pond snail Lymnaea stagnalis. Comp. Biochem. Physiol. B: Biochem. Mol. Biol. 137, 475–486 (2004). · DOI
- Yakubov, G. E., Papagiannopoulos, A., Rat, E., Easton, R. L. & Waigh, T. A. Molecular structure and rheological properties of short-side-chain heavily glycosylated porcine stomach mucin. Biomacromolecules 8, 3467–3477 (2007). · DOI
- Ballard, K. R., Klein, A. H., Hayes, R. A., Wang, T. & Cummins, S. F. The protein and volatile components of trail mucus in the Common Garden Snail, Cornu aspersum. PLoS ONE 16, e0251565 (2021). · DOI · Paper page
- Belouhova, M. et al. Microbial diversity of garden snail mucus. MicrobiologyOpen 11, e1263 (2022). · DOI · Paper page
- Tachapuripunya, V., Roytrakul, S., Chumnanpuen, P. & E-kobon, T. Unveiling putative functions of mucus proteins and their tryptic peptides in seven gastropod species using comparative proteomics and machine learning-based bioinformatics predictions. Molecules 26, 3475 (2021). · DOI · Paper page
- Jia, D. & Muthukumar, M. Theory of charged gels: swelling, elasticity, and dynamics. Gels 7, 49 (2021). · DOI
- Newar, J. & Ghatak, A. Studies on the adhesive property of snail adhesive mucus. Langmuir 31, 12155–12160 (2015). · DOI
- Cilia, G. & Fratini, F. Antimicrobial properties of terrestrial snail and slug mucus. J. Complementary Integrative Med. 15 (2018). · DOI
- Takagi, J. et al. Mucin O-glycans are natural inhibitors of Candida albicans pathogenicity. Nat. Chem. Biol. 18, 762–773 (2022). · DOI
- Greistorfer, S. et al. Snail mucus− glandular origin and composition in Helix pomatia. Zoology 122, 126–138 (2017). · DOI
- Sinitcyn, P., Rudolph, J. D. & Cox, J. Computational methods for understanding mass spectrometry-based shotgun proteomics data. Annu. Rev. Biomed. Data Sci. 1, 207–234 (2018). · DOI
- Rogers, L. D. & Overall, C. M. Proteolytic post-translational modification of proteins: proteomic tools and methodology. Mol. Cell Proteom. 12, 3532–3542 (2013). · DOI
- Espinosa, E. P., Koller, A. & Allam, B. Proteomic characterization of mucosal secretions in the eastern oyster, Crassostrea virginica. J. Proteom. 132, 63–76 (2016). · DOI
- Davidson, N. M., Hawkins, A. D. & Oshlack, A. SuperTranscripts: a data driven reference for analysis and visualisation of transcriptomes. Genome Biol. 18, 1–10 (2017). · DOI
- Kumar, S. et al. Genetic variants of mucins: unexplored conundrum. Carcinogenesis 38, 671–679 (2017).
- Hegde, P. S., White, I. R. & Debouck, C. Interplay of transcriptomics and proteomics. Curr. Opin. Biotechnol. 14, 647–651 (2003). · DOI
- Nicholas, B. et al. Shotgun proteomic analysis of human‐induced sputum. Proteomics 6, 4390–4401 (2006). · DOI
- Tørresen, O. K. et al. Tandem repeats lead to sequence assembly errors and impose multi-level challenges for genome and protein databases. Nucleic Acids Res. 47, 10994–11006 (2019). · DOI · Paper page
- Benedito, R. et al. The notch ligands Dll4 and Jagged1 have opposing effects on angiogenesis. Cell 137, 1124–1135 (2009). · DOI
- De Lau, W. B., Snel, B. & Clevers, H. C. The R-spondin protein family. Genome Biol. 13, 1–10 (2012). · DOI
- Gaur, R. K. Amino acid frequency distribution among eukaryotic proteins. IIOAB J. 5, 6 (2014).
- Lang, T. et al. Searching the evolutionary origin of epithelial mucus protein components-mucins and FCGBP. Mol. Biol. Evol. 33, 1921–1936 (2016). · DOI
- Li, D. & Graham, L. D. Epiphragmin, the major protein of epiphragm mucus from the vineyard snail, Cernuella virgata. Comp. Biochem. Physiol. B: Biochem. Mol. Biol. 148, 192–200 (2007). · DOI
- Mane, P. C. et al. Terrestrial snail-mucus mediated green synthesis of silver nanoparticles and in vitro investigations on their antimicrobial and anticancer activities. Sci. Rep. 11, 1–16 (2021). · DOI
- Li, Y., Su, J. & Cavaco-Paulo, A. Laccase-catalyzed cross-linking of BSA mediated by tyrosine. Int. J. Biol. Macromol. 166, 798–805 (2021). · DOI
- Park, S.-W. et al. The protein disulfide isomerase AGR2 is essential for production of intestinal mucus. Proc. Natl Acad. Sci. 106, 6950–6955 (2009). · DOI
- Provan, F. et al. Proteomic analysis of epidermal mucus from sea lice-infected Atlantic salmon, Salmo salar L. J. fish. Dis. 36, 311–321 (2013). · DOI
- Chen, Y. et al. FKBP65-dependent peptidyl-prolyl isomerase activity potentiates the lysyl hydroxylase 2-driven collagen cross-link switch. Sci. Rep. 7, 1–9 (2017). · DOI · Paper page
- Bilotto, P. et al. Adhesive properties of adsorbed layers of two recombinant mussel foot proteins with different levels of DOPA and Tyrosine. Langmuir 35, 15481–15490 (2019). · DOI
- Cao, W. et al. Unraveling the structure and function of melanin through synthesis. J. Am. Chem. Soc. 143, 2622–2637 (2021). · DOI
- Unlu, A. & Ekici, A. Phenoloxidase is involved in the immune reaction of Helix lucorum to parasitic infestation by dicrocoeliid trematode. Ann. Agric. Environ. Med. 28 (2021). · DOI
- Rajan, B. et al. Proteome reference map of the skin mucus of Atlantic cod (Gadus morhua) revealing immune competent molecules. Fish. Shellfish Immunol. 31, 224–231 (2011). · DOI
- Hasnain, S. Z., McGuckin, M. A., Grencis, R. K. & Thornton, D. J. Serine protease (s) secreted by the nematode Trichuris muris degrade the mucus barrier. PLoS Negl Trop Dis. 6, e1856(2012). · DOI
- Liu, W. et al. Stress-induced mucus secretion and its composition by a combination of proteomics and metabolomics of the Jellyfish Aurelia coerulea. Mar. Drugs 16, 341 (2018). · DOI
- Allain, T., Fekete, E. & Buret, A. G. Giardia cysteine proteases: the teeth behind the smile. Trends Parasitol. 35, 636–648 (2019). · DOI
- Nayak, A., Pednekar, L., Reid, K. B. & Kishore, U. Complement and non-complement activating functions of C1q: a prototypical innate immune molecule. Innate Immun. 18, 350–363 (2012). · DOI
- Pietrzyk-Brzezinska, A. J. & Bujacz, A. H-type lectins—structural characteristics and their applications in diagnostics, analytics and drug delivery. Int. J. Biol. Macromol. 152, 735–747 (2020). · DOI
- Caruana, N. J., Strugnell, J. M., Faou, P., Finn, J. & Cooke, I. R. Comparative proteomic analysis of slime from the striped pyjama squid, Sepioloidea lineolata, and the southern bottletail squid, Sepiadarium austrinum (Cephalopoda: Sepiadariidae). J. Proteome Res. 18, 890–899 (2019). · DOI
- Patel, D. M. & Brinchmann, M. F. Skin mucus proteins of lumpsucker (Cyclopterus lumpus). Biochem. Biophys. Rep. 9, 217–225 (2017).
- Johnson, M. et al. NCBI BLAST: a better web interface. Nucleic Acids Res. 36, W5–W9 (2008). · DOI
- El-Gebali, S. et al. The Pfam protein families database in 2019. Nucleic Acids Res. 47, D427–D432 (2019). · DOI · Paper page
- Moniaux, N., Escande, F., Porchet, N., Aubert, J.-P. & Batra, S. K. Structural organization and classification of the human mucin genes. Front. Biosci. 6, D1192–D1206 (2001). · DOI
- Crouzier, T. et al. Modulating mucin hydration and lubrication by deglycosylation and polyethylene glycol binding. Adv. Mater. Interfaces 2, 1500308 (2015). · DOI
- Wilkinson, H. & Saldova, R. Current methods for the characterization of O-glycans. J. Proteome Res. 19, 3890–3905 (2020). · DOI
- Stepan, H. et al. O-Glycosylation of snails. Glycoconj. J. 29, 189–198 (2012). · DOI
- Kang, P., Mechref, Y., Kyselova, Z., Goetz, J. A. & Novotny, M. V. Comparative glycomic mapping through quantitative permethylation and stable-isotope labeling. Anal. Chem. 79, 6064–6073 (2007). · DOI
- Jin, C. et al. Structural diversity of human gastric mucin glycans. Mol. Cell. Proteom. 16, 743–758 (2017). · DOI
- Jay, G. D. & Waller, K. A. The biology of lubricin: near frictionless joint motion. Matrix Biol. 39, 17–24 (2014). · DOI
- Wheeler, R. et al. Bacterial cell enlargement requires control of cell wall stiffness mediated by peptidoglycan hydrolases. MBio 6, e00660–00615 (2015). · DOI
- Valk-Weeber, R. L., Dijkhuizen, L. & van Leeuwen, S. S. Large-scale quantitative isolation of pure protein N-linked glycans. Carbohydr. Res. 479, 13–22 (2019). · DOI
- Staudacher, E. Mollusc N-glycosylation: structures, functions and perspectives. Biomolecules 11, 1820 (2021). · DOI
- Thomès, L. & Bojar, D. The role of fucose-containing glycan motifs across taxonomic kingdoms. Front. Mol. Biosci. 8, 755577 (2021). · DOI
- Staudacher, E. Mucin-type O-glycosylation in invertebrates. Molecules (Basel, Switz.) 20, 10622–10640 (2015). · DOI
- Shajahan, A., Supekar, N. T., Gleinich, A. S. & Azadi, P. Deducing the N- and O-glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2. Glycobiology 30, 981–988 (2020). · DOI
- Masmali, A. M., Purslow, C. & Murphy, P. J. The tear ferning test: a simple clinical technique to evaluate the ocular tear film. Clin. Exp. Optom. 97, 399–406 (2014). · DOI
- Danielsen, S. P. O. et al. Molecular characterization of polymer networks. Chem. Rev. 121, 5042–5092 (2021). · DOI
- Wu, G., Gotthardt, M. & Gollasch, M. Assessment of nanoindentation in stiffness measurement of soft biomaterials: kidney, liver, spleen and uterus. Sci. Rep. 10, 1–11 (2020). · DOI
- Fudge, D. S., Gardner, K. H., Forsyth, V. T., Riekel, C. & Gosline, J. M. The mechanical properties of hydrated intermediate filaments: insights from hagfish slime threads. Biophys. J. 85, 2015–2027 (2003). · DOI
- Wilks, A. M., Rabice, S. R., Garbacz, H. S., Harro, C. C. & Smith, A. M. Double-network gels and the toughness of terrestrial slug glue. J. Exp. Biol. 218, 3128–3137 (2015).
- Newar, J., Verma, S. & Ghatak, A. Effect of metals on underwater adhesion of gastropod adhesive mucus. ACS Omega 6, 15580–15589 (2021). · DOI
- Dastjerdi, A. K., Pagano, M., Kaartinen, M., McKee, M. & Barthelat, F. Cohesive behavior of soft biological adhesives: experiments and modeling. Acta Biomater. 8, 3349–3359 (2012). · DOI
- Picchioni, F. & Muljana, H. Hydrogels based on dynamic covalent and non covalent bonds: a chemistry perspective. Gels 4, 21 (2018). · DOI
- Zhao, X., Huebsch, N., Mooney, D. J. & Suo, Z. Stress-relaxation behavior in gels with ionic and covalent crosslinks. J. Appl. Phys. 107, 063509 (2010). · DOI
- Opell, B. D. & Stellwagen, S. D. Properties of orb weaving spider glycoprotein glue change during Argiope trifasciata web construction. Sci. Rep. 9, 1–11 (2019). · DOI
- Forsprecher, J., Wang, Z., Goldberg, H. A. & Kaartinen, M. T. Transglutaminase-mediated oligomerization promotes osteoblast adhesive properties of osteopontin and bone sialoprotein. Cell Adhes. Migr. 5, 65–72 (2011). · DOI
- Li, Y. & Chen, X. Sialic acid metabolism and sialyltransferases: natural functions and applications. Appl. Microbiol. Biotechnol. 94, 887–905 (2012). · DOI
- Figueroa-Morales, N., Dominguez-Rubio, L., Ott, T. L. & Aranson, I. S. Mechanical shear controls bacterial penetration in mucus. Sci. Rep. 9, 1–10 (2019). · DOI
- Pokki, J., Zisi, I., Schulman, E., Indana, D. & Chaudhuri, O. Magnetic probe-based microrheology reveals local softening and stiffening of 3D collagen matrices by fibroblasts. Biomed. Microdevices 23, 27 (2021). · DOI
- Guerardel, Y. et al. O-glycan variability of egg-jelly mucins from Xenopus laevis: characterization of four phenotypes that differ by the terminal glycosylation of their mucins. Biochem. J. 352, 449–463 (2000). · DOI
- Benktander, J. et al. Effects of size and geographical origin on Atlantic salmon, Salmo salar, Mucin O-Glycan Repertoire*[S]. Mol. Cell. Proteom. 18, 1183–1196 (2019). · DOI
- Kwan, C.-S., Cerullo, A. R. & Braunschweig, A. B. Design and synthesis of mucin-inspired glycopolymers. ChemPlusChem 85, 2704–2721 (2020). · DOI
- Lema, M. A. et al. Scalable preparation of synthetic mucins via nucleophilic ring-opening polymerization of glycosylated N-carboxyanhydrides. Macromolecules 55, 4710–4720 (2022). · DOI
- Corfield, A. P. Glycoprotein Methods and Protocols: The Mucins. Vol. 125 (Springer Science & Business Media, 2000). · DOI
- Kilcoyne, M., Gerlach, J. Q., Farrell, M. P., Bhavanandan, V. P. & Joshi, L. Periodic acid–Schiff’s reagent assay for carbohydrates in a microtiter plate format. Anal. Biochem. 416, 18–26 (2011). · DOI
- Dheilly, N. M. et al. A family of variable immunoglobulin and lectin domain containing molecules in the snail Biomphalaria glabrata. Dev. Comp. Immunol. 48, 234–243 (2015). · DOI
- Barcia, R., Lopez‐García, J. M. & Ramos‐Martínez, J. I. The 28S fraction of rRNA in molluscs displays electrophoretic behaviour different from that of mammal cells. IUBMB Life 42, 1089–1092 (1997). · DOI
- Brown, J., Pirrung, M. & McCue, L. A. FQC Dashboard: integrates FastQC results into a web-based, interactive, and extensible FASTQ quality control tool. Bioinformatics 33, 3137–3139 (2017). · DOI
- Bolger, A. M., Lohse, M. & Usadel, B. Trimmomatic: a flexible trimmer for Illumina sequence data. Bioinformatics 30, 2114–2120 (2014). · DOI · Paper page
- Haas, B. J. et al. De novo transcript sequence reconstruction from RNA-seq using the Trinity platform for reference generation and analysis. Nat. Protoc. 8, 1494–1512 (2013). · DOI · Paper page
- Helsens, K., Martens, L., Vandekerckhove, J. & Gevaert, K. MascotDatfile: an open‐source library to fully parse and analyse MASCOT MS/MS search results. Proteomics 7, 364–366 (2007). · DOI
- Searle, B. C. Scaffold: a bioinformatic tool for validating MS/MS‐based proteomic studies. Proteomics 10, 1265–1269 (2010). · DOI
- Perez-Riverol, Y. et al. The PRIDE database resources in 2022: a hub for mass spectrometry-based proteomics evidences. Nucleic Acids Res. 50, D543–D552 (2022). · DOI · Paper page
- Thompson, J. D., Gibson, T. J. & Higgins, D. G. Multiple sequence alignment using ClustalW and ClustalX. Curr. Protoc. Bioinformatcis Chapter 2, Unit 2.32.3 (2003).
- Duraisamy, S., Ramasamy, S., Kharbanda, S. & Kufe, D. Distinct evolution of the human carcinoma-associated transmembrane mucins, MUC1, MUC4 AND MUC16. Gene 373, 28–34 (2006). · DOI
- Letunic, I. & Bork, P. Interactive Tree Of Life (iTOL) v5: an online tool for phylogenetic tree display and annotation. Nucleic Acids Res. 49, W293–W296 (2021). · DOI
- Procter, J. B. et al. Alignment of Biological Sequences with Jalview. In Multiple Sequence Alignment. Methods in Molecular Biology (ed. Katoh, K.) vol 2231, 203–224 (Humana, New York, 2021). · DOI
- Bern, M., Kil, Y. J. & Becker, C. Byonic: advanced peptide and protein identification software. Curr. Protoc. Bioinform. 40, 13.20.11–13.20.14 (2012). · DOI · Paper page
- Burgess, S. & Pinard, P. AZtec wave—a necw way to achieve combined EDS and WDS capability on SEM. Microsc. Microanal. 26, 114–115 (2020). · DOI
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Hudz, N., Turkina, V., Alyokhina, T., Motyka, O., Chemerys, N., Rumynska, T., Lozynskyi, A., Jasicka-Misiak, I., & Kobylinska, L. (2025) · Molecules · doi:10.3390/molecules30214197 · Cited by 4
Metadata
- Authors
- Cerullo, A. R., McDermott, M. B., Pepi, L. E., Liu, Z.-L., Barry, D., Zhang, S., Yang, X., Chen, X., Azadi, P., Holford, M., & Braunschweig, A. B.
- Affiliations
- The Graduate Center, CUNY (US)
- Hunter College (US)
- University of Georgia (US)
- Corresponding author
- Braunschweig, Adam B.
- ORCID
- Venue
- Nature Communications
- Published
- 2023-09-02
- Volume
- 14
- Issue
- 1
- Pages
- 5361-5361
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC10475054
- OpenAlex
- W4386390645
- Cited by
- 35
- References
- 4
- Citations by year
- 2026: 7 · 2025: 16 · 2024: 6 · 2023: 6
- FWCI
- 2.39
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- United States Department of Defense | United States Air Force | AFMC | Air Force Office of Scientific Research (FA-9550-19-1-022-, FA9550-18-1-0142, FA9550-23-1-023)
- National Science Foundation (DMR-2212139, DMR-1933525)
- United States Department of Defense | United States Navy | Office of Naval Research (N00014-18-1-2492)
- U.S. Department of Health & Human Services | National Institutes of Health (R24GM137782)
- Topics
- Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Physical Sciences › Materials Science › Biomaterials › Hydrogels: synthesis, properties, applications
- Keywords
- Helix aspersa, mucus proteins, glycosylation, ion content, structure-function relationship
- MeSH terms
- Animals, Meat, Mucus, Hydrogels, Cornus, Gastropoda
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