Collagen Based Materials in Cosmetic Applications: A Review
Open accessAbstract
This review provides a report on properties and recent advances in the application of collagen in cosmetics. Collagen is a structural protein found in animal organisms where it provides for the fundamental structural support. Most commonly it is extracted from mammalian and fish skin. Collagen has attracted significant academic interest as well as the attention of the cosmetic industry due to its interesting properties that include being a natural humectant and moisturizer for the skin. This review paper covers the biosynthesis of collagen, the sources of collagen used in the cosmetic industry, and the role played by this protein in cosmetics. Future aspects regarding applications of collagen-based materials in cosmetics have also been mentioned.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Collagen from fish waste (skin, bones, scales) has nutraceutical, cosmeceutical, and biomedical applications because it is a source of many amino acids.
“Collagen from fish waste, such as skin, bones, and scales, has nutraceutical, cosmeceutical, and bio-medical applications because it is a source of many amino acids.”
From Use of Waste from the Food Industry and Applications of the Fermentation Process to Create Sustainable Cosmetic Products: A Review (2024) · cites this paper as [147]
Sections 3 and 4 identify fish skin, bones, and scales—including processing waste—as collagen sources, and section 10 says fish collagen is widely used in cosmetics. Section 7 discusses collagen peptides in nutraceuticals, and the review cites biomedical uses of fish-skin collagen, but it does not establish that all three applications arise because fish-waste collagen supplies many amino acids. Page numbers are unavailable in our copy. (LLM, conf=0.85)
Experimental — accuracy not yet measuredCollagen from fish waste possesses antioxidant, antimicrobial, and anti-aging properties desirable in cosmetics.
“It also possess antioxidant, antimicrobial, and anti-aging properties, which are highly desirable in the cosmetic industry [146,147].”
From Use of Waste from the Food Industry and Applications of the Fermentation Process to Create Sustainable Cosmetic Products: A Review (2024) · cites this paper as [147]
Section 7 says fish waste can be used to make collagen hydrolysates and describes hydrolyzed collagen as an antioxidant cosmetic ingredient. The Conclusions say collagen is used to prevent skin ageing. Neither passage establishes antimicrobial properties of fish-waste collagen, so that part of the claim is unsupported. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Chitin and chitosan: Properties and applications
Rinaudo, M. (2006) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2006.06.001 · Cited by 8,378 · see citing works
Ricard-Blum, S. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004978 · Cited by 2,305 · see citing works
The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development
Sorushanova, A., Delgado, L. M., Wu, Z., Shologu, N., Kshirsagar, A., Raghunath, R., Mullen, A. M., Bayon, Y., Pandit, A. S., Raghunath, M., et al. (2018) · Advanced Materials · doi:10.1002/adma.201801651 · Cited by 1,156 · see citing works
Current research on the blends of natural and synthetic polymers as new biomaterials: Review
Sionkowska, A. (2011) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2011.05.003 · Cited by 976 · see citing works
Self-citationGómez-Guillén, M. C., Turnay, J., Fernández-Díaz, M., Ulmo, N., Lizarbe, M. A., & Montero, P. (2002) · Food Hydrocolloids · doi:10.1016/s0268-005x(01)00035-2 · Cited by 847 · see citing works
Folk, J. E. (1980) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.49.070180.002505 · Cited by 838 · see citing works
Fibronectin fibrillogenesis, a cell-mediated matrix assembly process
Mao, Y., & Schwarzbauer, J. E. (2005) · Matrix Biology · doi:10.1016/j.matbio.2005.06.008 · Cited by 819 · see citing works
Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators
Kadler, K. E., Hill, A., & Canty‐Laird, E. G. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.06.008 · Cited by 757 · see citing works
Mechanisms of maturation and ageing of collagen
Bailey, A. J., Paul, R. G., & Knott, L. (1998) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(98)00119-5 · Cited by 672 · see citing works
Collagen: A review on its sources and potential cosmetic applications
Rodríguez, M. I. A., Barroso, L. G. R., & Sánchez, M. L. (2017) · Journal of Cosmetic Dermatology · doi:10.1111/jocd.12450 · Cited by 593 · see citing works
Hydrolyzed Collagen—Sources and Applications
León-López, A., Morales-Peñaloza, A., Juárez, V. M. M., Vargas‐Torres, A., Zeugolis, D. I., & Aguirre‐Álvarez, G. (2019) · Molecules · doi:10.3390/molecules24224031 · Cited by 562 · see citing works
Bone Morphogenetic Protein-1: The Type I Procollagen C-Proteinase
Kessler, E., Takahara, K., Biniaminov, L., Brusel, M., & Greenspan, D. S. (1996) · Science · doi:10.1126/science.271.5247.360 · Cited by 538 · see citing works
Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus)
Kittiphattanabawon, P., Benjakul, S., Visessanguan, W., Nagai, T., & Tanaka, M. (2004) · Food Chemistry · doi:10.1016/j.foodchem.2004.02.042 · Cited by 534 · see citing works
Molecular interactions in collagen and chitosan blends
Sionkowska, A., Wisniewski, M., Skopińska-Wiśniewska, J., et al. (2003) · Biomaterials · doi:10.1016/s0142-9612(03)00595-7 · Cited by 514 · see citing works
Self-citationGlutaraldehyde as a fixative in bioprostheses and drug delivery matrices
Jayakrishnan, A., & Jameela, S. R. (1996) · Biomaterials · doi:10.1016/0142-9612(96)82721-9 · Cited by 500 · see citing works
Marine Origin Collagens and Its Potential Applications
Silva, T. H., Moreira‐Silva, J., Marques, A. L. P., et al. (2014) · Marine Drugs · doi:10.3390/md12125881 · Cited by 454 · see citing works
Methods for the treatment of collagenous tissues for bioprostheses
Khor, E. (1997) · Biomaterials · doi:10.1016/s0142-9612(96)00106-8 · Cited by 416 · see citing works
Frohbergh, M. E., Katsman, A., Botta, G. P., Lazarovici, P., Schauer, C. L., Wegst, U. G. K., & Lelkes, P. I. (2012) · Biomaterials · doi:10.1016/j.biomaterials.2012.09.009 · Cited by 412 · see citing works
Modulation of Skin Collagen Metabolism in Aged and Photoaged Human Skin In Vivo
Chung, J. H., Seo, J. Y., Choi, H. R., Lee, M. K., Youn, C. S., Rhie, G., Cho, K. H., Kim, K. H., Park, K. C., & Eun, H. C. (2001) · Journal of Investigative Dermatology · doi:10.1046/j.0022-202x.2001.01544.x · Cited by 410 · see citing works
Enzyme-catalyzed gel formation of gelatin and chitosan: potential for in situ applications
Chen, T., Embree, H. D., Brown, E. M., Taylor, M. M., & Payne, G. F. (2003) · Biomaterials · doi:10.1016/s0142-9612(03)00096-6 · Cited by 359 · see citing works
Current methods of collagen cross-linking: Review
Adamiak, K., & Sionkowska, A. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.06.075 · Cited by 342 · see citing works
Self-citationAdverse reactions to injectable soft tissue fillers
Requena, L., Requena, C., Christensen, L. H., Zimmermann, U. S., Kutzner, H., & Cerroni, L. (2010) · Journal of the American Academy of Dermatology · doi:10.1016/j.jaad.2010.02.064 · Cited by 336 · see citing works
Engel, J. D., & Prockop, D. J. (1991) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.20.060191.001033 · Cited by 322 · see citing works
Biopolymers for hydrogels in cosmetics: review
Mitura, S., Sionkowska, A., & Jaiswal, A. K. (2020) · Journal of Materials Science Materials in Medicine · doi:10.1007/s10856-020-06390-w · Cited by 316 · see citing works
Self-citationZhang, Y., Liu, W., Li, G., Shi, B. Q., Miao, Y., & Wu, X. (2006) · Food Chemistry · doi:10.1016/j.foodchem.2006.09.053 · Cited by 264 · see citing works
Engel, J. (1991) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.20.1.137 · Cited by 264 · see citing works
Overview of skin aging and photoaging.
Helfrich, Y. R., Sachs, D. L., & Voorhees, J. J. (2008) · PubMed · Cited by 255 · see citing works
Addad, S., Exposito, J., Faye, C., et al. (2011) · Marine Drugs · doi:10.3390/md9060967 · Cited by 252 · see citing works
Genipin‐induced changes in collagen gels: Correlation of mechanical properties to fluorescence
Sundararaghavan, H. G., Monteiro, G. A., Lapin, N. A., Chabal, Y. J., Miksan, J. R., & Shreiber, D. I. (2008) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.31715 · Cited by 242 · see citing works
Zeugolis, D. I., Paul, G. R., & Attenburrow, G. (2008) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.32031 · Cited by 239 · see citing works
Park, S.-N., Lee, H. J., Lee, K. H., & Suh, H. (2003) · Biomaterials · doi:10.1016/s0142-9612(02)00550-1 · Cited by 238 · see citing works
Collagen of the skin of ocellate puffer fish (Takifugu rubripes)
Nagai, T., Araki, Y., & Suzuki, N. (2002) · Food Chemistry · doi:10.1016/s0308-8146(01)00396-x · Cited by 230 · see citing works
Cosmetic Potential of Marine Fish Skin Collagen
Alves, A. L. D. S., Marques, A., Martins, E., Silva, T. H., & Reis, R. L. (2017) · Cosmetics · doi:10.3390/cosmetics4040039 · Cited by 225 · see citing works
Hsp47: a molecular chaperone that interacts with and stabilizes correctly‐folded procollagen
Tasab, M., Batten, M. R., & Bulleid, N. J. (2000) · The EMBO Journal · doi:10.1093/emboj/19.10.2204 · Cited by 223 · see citing works
Goodarzi, H., Jadidi, K., Pourmotabed, S., Sharifi, E., & Aghamollaei, H. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.12.125 · Cited by 221 · see citing works
Isolation and characterization of collagen from brown backed toadfish (Lagocephalus gloveri) skin
Senaratne, L. S., Park, P., & Kim, S. (2005) · Bioresource Technology · doi:10.1016/j.biortech.2005.02.024 · Cited by 219 · see citing works
Collagen Hydrolysates for Skin Protection: Oral Administration and Topical Formulation
Aguirre-Cruz, G., León-López, A., Cruz-Gómez, V., Jiménez-Alvarado, R., & Aguirre‐Álvarez, G. (2020) · Antioxidants · doi:10.3390/antiox9020181 · Cited by 218 · see citing works
Intracellular Steps in the Biosynthesis of Collagen
Prockop, D. J., Berg, R. A., Kivirikko, K. I., & Uitto, J. (1976) · Springer eBooks · doi:10.1007/978-1-4757-4602-0_5 · Cited by 214 · see citing works
Nagai, T., Yamashita, E., Taniguchi, K., Kanamori, N., & Suzuki, N. (2001) · Food Chemistry · doi:10.1016/s0308-8146(00)00249-1 · Cited by 202 · see citing works
The review of versatile application of collagen
Sionkowska, A., Skrzyński, S., Śmiechowski, K., & Kołodziejczak, A. (2016) · Polymers for Advanced Technologies · doi:10.1002/pat.3842 · Cited by 191 · see citing works
Self-citationZhang, M., Liu, W., & Li, G. (2009) · Food Chemistry · doi:10.1016/j.foodchem.2009.01.006 · Cited by 184 · see citing works
Injectable fillers for facial rejuvenation: a review
Buck, D. W., Alam, M., & Kim, J. Y. S. (2008) · Journal of Plastic Reconstructive & Aesthetic Surgery · doi:10.1016/j.bjps.2008.06.036 · Cited by 181 · see citing works
Collagen and its interaction with chitosan
Taravel, M. N., & Domard, A. (1995) · Biomaterials · doi:10.1016/0142-9612(95)94149-f · Cited by 168 · see citing works
Isolation and characterization of collagen from rhizostomous jellyfish (Rhopilema asamushi)
Nagai, T., Worawattanamateekul, W., Suzuki, N., et al. (2000) · Food Chemistry · doi:10.1016/s0308-8146(00)00081-9 · Cited by 162 · see citing works
Bhagwat, P. K., & Dandge, P. B. (2016) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2016.06.010 · Cited by 149 · see citing works
STRUCTURAL AND CHEMICAL STUDIES ON THE CONNECTIVE TISSUE OF MARINE SPONGES
Gross, J., SOKAL, Z., & Rougvie, M. A. (1956) · Journal of Histochemistry & Cytochemistry · doi:10.1177/4.3.227 · Cited by 148 · see citing works
Carvalho, A. M., Marques, A. P., Silva, T. H., & Reis, R. L. (2018) · Marine Drugs · doi:10.3390/md16120495 · Cited by 146 · see citing works
Oliveira, V. D. M., Assis, C. R. D., da Costa, B. D. A. M., Neri, R. C. A., do Monte, F. T. D., Freitas, H. M. S. D. C. V., França, R. C. P., dos Santos, J. F., Bezerra, R. D. S., & Porto, T. S. (2020) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2020.129023 · Cited by 144 · see citing works
Delayed Triple Helix Formation of Mutant Collagen from Patient with Osteogenesis Imperfecta
Raghunath, M., Brückner, P., & Steinmann, B. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1199 · Cited by 139 · see citing works
Diverse biological functions of extracellular collagen processing enzymes
Trackman, P. C. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20605 · Cited by 134 · see citing works
Collagen Cryogel Cross‐Linked by Dialdehyde Starch
Mu, C., Liu, F., Cheng, Q., Li, H., Wu, B., Zhang, G., & Lin, W. J. (2010) · Macromolecular Materials and Engineering · doi:10.1002/mame.200900292 · Cited by 129 · see citing works
Li, J., Wang, M., Qiao, Y., Tian, Y., Liu, J., Qin, S., & Wu, W. (2018) · Process Biochemistry · doi:10.1016/j.procbio.2018.07.009 · Cited by 122 · see citing works
Enzymatic Hydrolysis of Fish Waste as an Alternative to Produce High Value-Added Products
Araujo, J., Sica, P., Costa, C., et al. (2020) · Waste and Biomass Valorization · doi:10.1007/s12649-020-01029-x · Cited by 117 · see citing works
Ultrastructural Studies on the Collagen of the Marine Sponge Chondrosia reniformis Nardo
Heinemann, S., Ehrlich, H., Douglas, T., Heinemann, C., Worch, H., Schatton, W. F. H., & Hanke, T. (2007) · Biomacromolecules · doi:10.1021/bm700574y · Cited by 110 · see citing works
Human skin collagen. Presence of type I and type III at all levels of the dermis.
Epstein, E. H., & Munderloh, N. H. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34870-6 · Cited by 109 · see citing works
Modification of collagen and chitosan mixtures by the addition of tannic acid
Sionkowska, A., Kaczmarek, B., & Lewandowska, K. (2014) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2014.09.028 · Cited by 108 · see citing works
Self-citationStability and mobility of the collagen structure
Privalov, P. L., Tiktopulo, E. I., & Tischenko, V. M. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90240-7 · Cited by 108 · see citing works
Induction of angiogenesis using VEGF releasing genipin-crosslinked electrospun gelatin mats
Gaudio, C. D., Baiguera, S., Boieri, M., Mazzanti, B., Ribatti, D., Bianco, A., & Macchiarini, P. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.06.040 · Cited by 107 · see citing works
Song, W., Liu, D., Sun, L., Li, B., & Hou, H. (2019) · Marine Drugs · doi:10.3390/md17030137 · Cited by 107 · see citing works
Tziveleka, L., Ioannou, E., Tsiourvas, D., Berillis, P., Foufa, E., & Roussis, V. (2017) · Marine Drugs · doi:10.3390/md15060152 · Cited by 105 · see citing works
Miura, S., & Kimura, S. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)95743-1 · Cited by 104 · see citing works
Secchi, G. (2008) · Clinics in Dermatology · doi:10.1016/j.clindermatol.2008.04.004 · Cited by 100 · see citing works
Lysyl Hydroxylase 3-mediated Glucosylation in Type I Collagen
Sricholpech, M., Perdivara, I., Yokoyama, M., Nagaoka, H., Terajima, M., Tomer, K. B., & Yamauchi, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.343954 · Cited by 99 · see citing works
New Gelatin-Based Hydrogels via Enzymatic Networking
Crescenzi, V., Francescangeli, A., & Taglienti, A. (2002) · Biomacromolecules · doi:10.1021/bm025657m · Cited by 99 · see citing works
Microstructure, rheological and wound healing properties of collagen-based gel from cuttlefish skin
Jridi, M., Bardaa, S., Moalla, D., et al. (2015) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.03.020 · Cited by 96 · see citing works
Dual Crosslinked Collagen/Chitosan Film for Potential Biomedical Applications
Shah, R., Stodůlka, P., Skopalová, K., & Sáha, P. (2019) · Polymers · doi:10.3390/polym11122094 · Cited by 89 · see citing works
Li, G. Y., Fukunaga, S., Takenouchi, K., et al. (2005) · International Journal of Cosmetic Science · doi:10.1111/j.1467-2494.2004.00251.x · Cited by 87 · see citing works
Sionkowska, A., Michalska‐Sionkowska, M., & Walczak, M. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.01.262 · Cited by 87 · see citing works
Self-citationThermal and mechanical properties of UV irradiated collagen/chitosan thin films
Sionkowska, A., Wiśniewski, M., Skopińska-Wiśniewska, J., et al. (2006) · Polymer Degradation and Stability · doi:10.1016/j.polymdegradstab.2006.08.009 · Cited by 84 · see citing works
Self-citationTwo Stage Process for Dialdehyde Starch Using Electrolytic Regeneration of Periodic Acid
Pfeifer, V. F., Sohns, V. E., Conway, H. F., et al. (1960) · Industrial & Engineering Chemistry · doi:10.1021/ie50603a020 · Cited by 84 · see citing works
Interaction of collagen and poly(vinyl pyrrolidone) in blends
Sionkowska, A. (2003) · European Polymer Journal · doi:10.1016/s0014-3057(03)00161-7 · Cited by 84 · see citing works
Self-citationCharacterisation of acid-soluble collagen from skin of silver carp (Hypophthalmichthys molitrix)
Zhang, J., Duan, R., Tian, Y., & Konno, K. (2009) · Food Chemistry · doi:10.1016/j.foodchem.2009.02.053 · Cited by 82 · see citing works
Chotphruethipong, L., Battino, M. A., & Benjakul, S. (2020) · Food Chemistry · doi:10.1016/j.foodchem.2020.127127 · Cited by 81 · see citing works
Junqua, S., Robert, L., Garrone, R., et al. (1974) · Connective Tissue Research · doi:10.3109/03008207409152244 · Cited by 77 · see citing works
Surface and thermal properties of collagen/hyaluronic acid blends containing chitosan
Lewandowska, K., Sionkowska, A., Grabska-Zielińska, S., et al. (2016) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2016.07.055 · Cited by 76 · see citing works
Self-citationGarcia, Y., Naik, H., Collighan, R. J., et al. (2008) · Tissue Engineering Part A · doi:10.1089/ten.tea.2008.0104 · Cited by 73 · see citing works
Grabska-Zielińska, S., Sionkowska, A., Reczyńska-Kolman, K., & Pamuła, E. (2020) · Polymers · doi:10.3390/polym12020372 · Cited by 72 · see citing works
Self-citationSionkowska, A., Kaczmarek, B., Michalska, M., Lewandowska, K., & Grabska-Zielińska, S. (2017) · Pure and Applied Chemistry · doi:10.1515/pac-2017-0314 · Cited by 71 · see citing works
Self-citationQuality control in the endoplasmic reticulum
Bottomley, M. J., Batten, M. R., Lumb, R. A., et al. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00317-7 · Cited by 70 · see citing works
Thermal and Rheological Behavior of Collagen. Chitosan blends
Machado, A. A. S., Martins, V. D. C. A., & Plepis, A. M. D. G. (2002) · Journal of Thermal Analysis and Calorimetry · doi:10.1023/a:1013953316829 · Cited by 69 · see citing works
Assessment of cell viability in a three-dimensional enzymatically cross-linked collagen scaffold
Garcia, Y., Collighan, R. J., Griffin, M., & Pandit, A. S. (2007) · Journal of Materials Science Materials in Medicine · doi:10.1007/s10856-007-3091-9 · Cited by 67 · see citing works
Collagen Content in Farmed Atlantic Salmon (Salmo salarL.)
Aidos, I., Lie, Ø. H., & Espe, M. (1999) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf980761+ · Cited by 66 · see citing works
Lewandowska, K., Sionkowska, A., Grabska-Zielińska, S., Kaczmarek, B., & Michalska, M. (2016) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2016.05.009 · Cited by 64 · see citing works
Self-citationISOLATION AND CHARACTERIZATION OF COLLAGENS FROM SCALE OF SILVER CARP (HYPOPHTHALMICHTHYS MOLITRIX)
Zhang, J., Duan, R., YE, C., & Konno, K. (2010) · Journal of Food Biochemistry · doi:10.1111/j.1745-4514.2010.00439.x · Cited by 63 · see citing works
Pallela, R., Sreedhar, B., & Janapala, V. R. (2011) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2011.03.019 · Cited by 62 · see citing works
An improved method to prepare hyaluronic acid and type II collagen composite matrices
Taguchi, T., Ikoma, T., & Tanaka, J. (2002) · Journal of Biomedical Materials Research · doi:10.1002/jbm.10147 · Cited by 61 · see citing works
Yan, J., Li, X., Liu, L., Wang, F., Zhu, T. W., & Zhang, Q. (2006) · Artificial Cells Blood Substitutes and Biotechnology · doi:10.1080/10731190500430024 · Cited by 55 · see citing works
Use of Chitosan as a Bioactive Implant Coating for Bone-Implant Applications
Leedy, M. R., Martin, H. J., Norowski, P. A., Jennings, J. A., Haggard, W. O., & Bumgardner, J. D. (2011) · Advances in polymer science · doi:10.1007/12_2011_115 · Cited by 53 · see citing works
Collagen as the Major Edible Component of Jellyfish ( Stomolophus nomural )
KIMURA, S., MIURA, S., & Park, Y. J. (1983) · Journal of Food Science · doi:10.1111/j.1365-2621.1983.tb05078.x · Cited by 53 · see citing works
Koide, T., & Nagata, K. (2005) · Topics in current chemistry · doi:10.1007/b103820 · Cited by 53 · see citing works
Evaluation for collagen products for cosmetic application
Peng, Y., Glattauer, V., Werkmeister, J. A., et al. (2004) · International Journal of Cosmetic Science · doi:10.1111/j.1467-2494.2004.00245_2.x · Cited by 50 · see citing works
Genipin, a Cross-linking Agent, Promotes Odontogenic Differentiation of Human Dental Pulp Cells
Kwon, Y.-S., Lim, E.-S., Kim, H.-M., Hwang, Y., Lee, K., & Min, K. (2015) · Journal of Endodontics · doi:10.1016/j.joen.2014.12.002 · Cited by 49 · see citing works
Collagen–synthetic polymer interactions in solution and in thin films
Sionkowska, A., Skopińska-Wiśniewska, J., & Wiśniewski, M. (2008) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2008.06.005 · Cited by 48 · see citing works
Self-citationIsolation and Biochemical Characterisation of a Novel Collagen from Catostylus tagi
Calejo, M. T., Morais, Z., & Fernandes, A. I. (2009) · Journal of Biomaterials Science Polymer Edition · doi:10.1163/156856208x399125 · Cited by 48 · see citing works
Review of soft tissue augmentation in the face
Newman, J. P. (2009) · Clinical Cosmetic and Investigational Dermatology · doi:10.2147/ccid.s3631 · Cited by 48 · see citing works
Mechanical property and biocompatibility of silk fibroin–collagen type II composite membrane
Lin, X., Gao, L., Li, R., et al. (2019) · Materials Science and Engineering C · doi:10.1016/j.msec.2019.110018 · Cited by 47 · see citing works
Miscibility studies on the blends of collagen/chitosan by dilute solution viscometry
Ye, Y., Dan, W., Zeng, R., et al. (2007) · European Polymer Journal · doi:10.1016/j.eurpolymj.2006.10.024 · Cited by 46 · see citing works
Rodziewicz‐Motowidło, S., Śladewska, A., Mulkiewicz, E., et al. (2008) · Aquaculture · doi:10.1016/j.aquaculture.2008.08.026 · Cited by 45 · see citing works
Campos, P. M. B. G. M., de Melo, M. O., & César, F. C. S. (2019) · Journal of Cosmetic Dermatology · doi:10.1111/jocd.12893 · Cited by 45 · see citing works
Isolation and biochemical characterization of collagens from seaweed pipefish, Syngnathus schlegeli
Khan, S. B., Qian, Z., Ryu, B., et al. (2009) · Biotechnology and Bioprocess Engineering · doi:10.1007/s12257-009-0007-1 · Cited by 41 · see citing works
Beneficial effects of food supplements based on hydrolyzed collagen for skin care (Review)
Lupu, M., Pîrcălăbioru, G. G., Chifiriuc, M. C., Albulescu, R., & Tănase, C. (2019) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2019.8342 · Cited by 41 · see citing works
Biodegradable packing materials based on waste collagen hydrolysate cured with dialdehyde starch
Langmaier, F., Mládek, M., Mokrejš, P., et al. (2008) · Journal of Thermal Analysis and Calorimetry · doi:10.1007/s10973-007-8293-3 · Cited by 38 · see citing works
Chung, E. J., Jakus, A. E., & Shah, R. N. (2012) · Acta Biomaterialia · doi:10.1016/j.actbio.2012.09.021 · Cited by 38 · see citing works
Collagen of octopus Callistoctopus arakawai arm
Nagai, T., Nagamori, K., Yamashita, E., et al. (2002) · International Journal of Food Science & Technology · doi:10.1046/j.1365-2621.2002.00568.x · Cited by 37 · see citing works
Ghaeli, I., de Moraes, M. A., Beppu, M. M., et al. (2017) · Molecules · doi:10.3390/molecules22081368 · Cited by 37 · see citing works
Gong, Z., Xiong, H., Long, X., et al. (2010) · Biomedical Materials · doi:10.1088/1748-6041/5/5/055005 · Cited by 36 · see citing works
Nomura, Y., Toki, S., Ishii, Y., & SHIRAI, K. (2000) · Biomacromolecules · doi:10.1021/bm000085w · Cited by 33 · see citing works
Wei, P., Zheng, H. S., Shi, Z., Li, D., & Xiang, Y.-L. (2019) · Journal of Wuhan University of Technology-Mater Sci Ed · doi:10.1007/s11595-019-2143-6 · Cited by 31 · see citing works
Collagen from Diamondback Squid (Thysanoteuthis rhombus) Outer Skin
Nagai, T. (2004) · Zeitschrift für Naturforschung C · doi:10.1515/znc-2004-3-426 · Cited by 29 · see citing works
MILLER, A. T., Karmas, E., & LU, M. F. (1983) · Journal of Food Science · doi:10.1111/j.1365-2621.1983.tb14875.x · Cited by 28 · see citing works
Cellular response to collagen-elastin composite materials
Bax, D. V., Smalley, H. E., Farndale, R. W., et al. (2018) · Acta Biomaterialia · doi:10.1016/j.actbio.2018.12.033 · Cited by 28 · see citing works
Stability studies of collagen-based microspheres with Calendula officinalis flower extract
Kozłowska, J., Stachowiak, N., & Prus-Walendziak, W. (2019) · Polymer Degradation and Stability · doi:10.1016/j.polymdegradstab.2019.03.015 · Cited by 28 · see citing works
Fluorescence of Muscle and Connective Tissue from Cod and Salmon
Andersen, C. M., & Wold, J. P. (2002) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf020524d · Cited by 27 · see citing works
Wang, Y., McAllister, T. A., Xu, Z. J., Gruber, M. Y., Skadhauge, B., Jende‐Strid, B., & Cheng, K. J. (1999) · Journal of the Science of Food and Agriculture · doi:10.1002/(sici)1097-0010(19990501)79:6 · Cited by 26 · see citing works
Study on the preparation of collagen-modified silk fibroin films and their properties
Tang, Y., Cao, C., Ma, X., et al. (2006) · Biomedical Materials · doi:10.1088/1748-6041/1/4/010 · Cited by 24 · see citing works
Niculescu, M. D., Epure, D. G., Lasoń-Rydel, M., et al. (2019) · The EuroBiotech Journal · doi:10.2478/ebtj-2019-0019 · Cited by 24 · see citing works
Non–animal collagens as new options for cosmetic formulation
Peng, Y. Y., Stoichevska, V., Vashi, A. V., et al. (2015) · International Journal of Cosmetic Science · doi:10.1111/ics.12243 · Cited by 17 · see citing works
Polymer films based on silk fibroin and collagen - the physico-chemical properties
Sionkowska, A., Grabska-Zielińska, S., Lewandowska, K., et al. (2016) · Molecular Crystals and Liquid Crystals · doi:10.1080/15421406.2016.1255084 · Cited by 15 · see citing works
Self-citationNagelschmidt, M., & Struck, H. (1974) · Archives of Dermatological Research · doi:10.1007/bf00561190 · Cited by 13 · see citing works
A cortical cytoskeleton in expanded epithelium cells of sponge gemmules
BRØNDSTED, H. V., & Carlsen, F. (1951) · Experimental Cell Research · doi:10.1016/0014-4827(51)90008-0 · Cited by 11 · see citing works
Quality attributes of partially hydrolyzed collagen in a liquid formulation used for skin care
Mejía‐Calvo, I., López‐Juárez, L. E., Vázquez‐Leyva, S., et al. (2020) · Journal of Cosmetic Dermatology · doi:10.1111/jocd.13439 · Cited by 8 · see citing works
[Collagen as cosmetic compound? (author's transl)].
Nagelschmidt, M., & Struck, H. (1974) · PubMed · Cited by 1 · see citing works
Flagged first, then by citations
Research works printed but not linked: 7
- [46]Fielding A.M. Preparation of neutral salt soluble collagen The Methodology of Connective Tissue Research 1st ed. Hall D.A. Joynson-Bruvvers Oxford, UK 1976 9 12
- [47]Trelstad R. Immunochemistry of the Extracellular Matrix 1st ed. CRC Press Boca Raton, FL, USA 1982
- [48]Piez K. Reddi K. Extracellular Matrix Biochemistry 1st ed. Elsevier New York, NY, USA 1984
- [50]Ervin H. Epstein J. Munderloh N. Human skin collagen J. Biol. Chem. 1978 253 1336 1337 342524
- [61]Nagelschmidt M. Struck H. Collagen as cosmetic compound? Arch. Dermatol. Res. 1974 250 237 243 4138565
- [68]DeVore D. Kelman C. Fagien S. Casson P. Autologen: Autologous, injectable, dermal collagen Principles and Practice of Ophthalmic Plastic and Reconstructive Surgery Bosniak S.W.B. Saunders Philadelphia, PA, USA 1996 670 675
- [75]León-López A. Morales-Peñaloza A. Martínez-Juárez V.M. Vargas-Torres A. Zeugolis D.I. Aguirre-Álvarez G. Hydrolyzed collagen—Sources and applications Molecules 2019 24 4031 10.3390/molecules24224031 PMC6891674 31703345 · DOI
Cited by
Sorted by citations
Fertala, A. (2020) · Bioengineering · doi:10.3390/bioengineering7040155 · Cited by 109 · see citing works
Krzyżostan, M., Wawrzyńczak, A., & Nowak, I. (2024) · Sustainability · doi:10.3390/su16072757 · Cited by 47 · see citing works
“Biohydrogen, bioethanol, and biogas are also produced from waste of fruits and vegetables containing starch, cellulose, and hemicelluloses, which are at first hydrolysed to soluble sugars and further fermented [148,149].”
Trends in biopolymer science applied to cosmetics
Mendoza‐Muñoz, N., Leyva‐Gómez, G., Piñón‐Segundo, E., Zambrano‐Zaragoza, M. L., Quintanar‐Guerrero, D., Del Prado Audelo, M. L., & Urbán‐Morlán, Z. (2023) · International Journal of Cosmetic Science · doi:10.1111/ics.12880 · Cited by 42 · see citing works
Chutoprapat, R., Witarat, J., Jongpanyangarm, P., Mang Sung Thluai, L., Khankaew, P., & Wah Chan, L. (2024) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2024.123980 · Cited by 11 · see citing works
- Authors
- Sionkowska, A., Adamiak, K., Musiał, K., & Gadomska, M.
- Affiliations
- Nicolaus Copernicus University (PL)
- Corresponding author
- Sionkowska, Alina
- Venue
- Materials
- Publisher
- MDPI AG
- Published
- 2020-09-23
- Volume
- 13
- Issue
- 19
- Pages
- 4217
- ISSN
- 1996-1944 (ISSN-L)
- PMC
- PMC7578929
- OpenAlex
- W3089149564
- Cited by
- 198
- References
- 122
- Citations by year
- 2026: 24 · 2025: 35 · 2024: 44 · 2023: 43 · 2022: 31 · 2021: 18 · 2020: 2
- FWCI
- 1.57
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Materials (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Health Sciences › Medicine › Dermatology › Skin Protection and Aging
- Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
- Keywords
- collagen, cosmetic applications, collagen-based materials, collagen extraction, fish skin collagen, humectants, skin hydration, collagen synthesis, structural proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review