{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,9]],"date-time":"2026-09-09T14:09:19Z","timestamp":1788962959911,"version":"build-2803163510"},"reference-count":61,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2021,12,29]],"date-time":"2021-12-29T00:00:00Z","timestamp":1640736000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100006595","name":"Unitatea Executiva Pentru Finantarea Invatamantului Superior a Cercetarii Dezvoltarii si Inovarii","doi-asserted-by":"publisher","award":["PN-III-P2-2.1-PED-2016-0187"],"award-info":[{"award-number":["PN-III-P2-2.1-PED-2016-0187"]}],"id":[{"id":"10.13039\/501100006595","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Riboflavin under UVA radiation generates reactive oxygen species (ROS) that can induce various changes in biological systems. Under controlled conditions, these processes can be used in some treatments for ocular or dermal diseases. For instance, corneal cross-linking (CXL) treatment of keratoconus involves UVA irradiation combined with riboflavin aiming to induce the formation of new collagen fibrils in cornea. To reduce the damaging effect of ROS formed in the presence of riboflavin and UVA, the CXL treatment is performed with the addition of polysaccharides (dextran). Hyaluronic acid is a polysaccharide that can be found in the aqueous layer of the tear film. In many cases, keratoconus patients also present dry eye syndrome that can be reduced by the application of topical solutions containing hyaluronic acid. This study presents physico-chemical evidence on the effect of riboflavin on collagen fibril formation revealed by the following methods: differential scanning microcalorimetry, rheology, and STEM images. The collagen used was extracted from calf skin that contains type I collagen similar to that found in the eye. Spin trapping experiments on collagen\/hyaluronic acid\/riboflavin solutions evidenced the formation of ROS species by electron paramagnetic resonance measurements.<\/jats:p>","DOI":"10.3390\/molecules27010190","type":"journal-article","created":{"date-parts":[[2021,12,29]],"date-time":"2021-12-29T08:12:15Z","timestamp":1640765535000},"page":"190","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Model Systems for Evidencing the Mediator Role of Riboflavin in the UVA Cross-Linking Treatment of Keratoconus"],"prefix":"10.3390","volume":"27","author":[{"given":"Mihaela Monica","family":"Constantin","sequence":"first","affiliation":[{"name":"Oftaclinic Clinic, Bd. 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J. Ophthalmol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1111\/j.1755-3768.2011.02369.x","article-title":"Proteases, proteolysis and inflammatory molecules in the tears of people with keratoconus","volume":"90","author":"Balasubramanian","year":"2012","journal-title":"Acta Ophthalmol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.3109\/02713683.2014.987871","article-title":"Signs and symptoms of dry eye in keratoconus patients: A pilot study","volume":"40","author":"Carracedo","year":"2015","journal-title":"Curr. Eye Res."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"620","DOI":"10.1016\/S0002-9394(02)02220-1","article-title":"Riboflavin\/ultraviolet-A\u2013induced collagen crosslinking for the treatment of keratoconus","volume":"135","author":"Wollensak","year":"2003","journal-title":"Am. J. Ophathalmol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/j.optom.2013.12.001","article-title":"Corneal collagen cross-linking: A review","volume":"7","year":"2014","journal-title":"J. Optom."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1113","DOI":"10.1111\/j.1524-4725.2011.02047.x","article-title":"Photoinduced collagen cross-linking: A new approach to venous insufficiency","volume":"37","author":"Frullini","year":"2011","journal-title":"Dermatol. Surg."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1007\/s00223-017-0343-7","article-title":"Effects of collagen crosslinkers on dentine: A literature review","volume":"102","author":"Cai","year":"2018","journal-title":"Calcif. Tissue Int."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1006\/exer.1997.0410","article-title":"Induction of cross-links in corneal tissue","volume":"66","author":"Spoerl","year":"1998","journal-title":"Exp. Eye Res."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1111\/j.1600-0420.2005.00447.x","article-title":"Cross-linking of scleral collagen in the rabbit using riboflavin and UVA","volume":"83","author":"Wollensak","year":"2005","journal-title":"Acta Ophthalmol. Scand."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1080\/02713680490513182","article-title":"Increased resistance of crosslinked cornea against enzymatic digestion","volume":"29","author":"Spoerl","year":"2004","journal-title":"Curr. Eye Res."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1007\/164_2016_23","article-title":"Keratoconus and other corneal diseases: Pharmacologic cross-linking and future therapy","volume":"242","author":"Hsu","year":"2017","journal-title":"Pharm. Log. Ther. Ocul. Dis."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1039\/C8AY02783H","article-title":"Spin probe method of electron paramagnetic resonance spectroscopy-a qualitative test for measuring the evolution of dry eye syndrome under treatment","volume":"11","author":"Constantin","year":"2019","journal-title":"Anal. Methods"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.exer.2011.12.010","article-title":"Levels of lactoferrin, secretory IgA and serum albumin in the tear film of people with keratoconus","volume":"96","author":"Balasubramanian","year":"2012","journal-title":"Exp. Eye Res."},{"key":"ref_14","first-page":"3100","article-title":"Tear lipocalins: Potential lipid scavengers for the corneal surface","volume":"40","author":"Glasgow","year":"1999","journal-title":"Investig. Ophthalmol. Vis. Sci."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.cca.2005.12.035","article-title":"Laboratory findings in tear fluid analysis","volume":"369","author":"Ohashi","year":"2006","journal-title":"Clin. Chim. Acta"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1038\/eye.1989.64","article-title":"The ocular surface in keratoconjunctivitis sicca","volume":"3","author":"Bron","year":"1989","journal-title":"Eye"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1038\/eye.1987.34","article-title":"Structure, function and ageing of the collagens of the eye","volume":"1","author":"Bailey","year":"1987","journal-title":"Eye"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/j.jsamd.2021.02.001","article-title":"Advanced collagen nanofibers-based functional bio-composites for high-value utilization of leather: A review","volume":"6","author":"Wang","year":"2021","journal-title":"J. Sci. Adv. Mater. Devices"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"6578","DOI":"10.1016\/S0021-9258(19)46970-6","article-title":"Collagen fibril formation: Optimal in vitro conditions and preliminary kintic results","volume":"253","author":"Williams","year":"1978","journal-title":"J. Biol. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"4973","DOI":"10.1016\/S0021-9258(19)69353-1","article-title":"Type I collagen fibrillogenesis in vitro: Additional evidence for the assembly mechanism","volume":"256","author":"Silver","year":"1981","journal-title":"J. Biol. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1016\/S0174-173X(83)80020-X","article-title":"Kinetic analysis of collagen fibrillogenesis: I. Use of turbidity-time data","volume":"3","author":"Silver","year":"1983","journal-title":"Collagen Rel. Res."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0174-173X(84)80034-5","article-title":"Kinetic analysis of collagen fibrillogenesis: II. Corneal and scleral type I collagen","volume":"4","author":"Birk","year":"1984","journal-title":"Collagen Rel. Res."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"37352","DOI":"10.1074\/jbc.M304325200","article-title":"Macromolecular specificity of collagen fibrillogenesis: Fibrils of collagens I and XI contain a heteritypic alloyed core and a collagen I sheath","volume":"278","author":"Hansen","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_24","first-page":"1509","article-title":"Fibrillogenesis in dense collagen solutions: A physicochemical study","volume":"376","author":"Gobeaux","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_25","first-page":"122","article-title":"Segregation of type I collagen homo- and heterotrimers in fibrils","volume":"383","author":"Han","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1999","DOI":"10.3762\/bjoc.10.208","article-title":"Photo, thermal and chemical degradation of riboflavin","volume":"10","author":"Sheraz","year":"2014","journal-title":"Beilstein J. Org. Chem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"94","DOI":"10.3109\/03009737709179078","article-title":"Interaction between cells, hyaluronic acid and collagen","volume":"82","author":"Balazs","year":"1977","journal-title":"Upsala J. Med. Sci."},{"key":"ref_28","first-page":"419","article-title":"Photodegradation of hyaluronic acid and of the vitreous body","volume":"9","author":"Lapcik","year":"1990","journal-title":"Gen. Physiol. Biophys."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"269","DOI":"10.3109\/03008208609001985","article-title":"Differences in the fibril structure of corneal and tendon collagen. An electron microscopy and X-ray diffraction investigation","volume":"15","author":"Marchini","year":"1986","journal-title":"Connect. Tissue Res."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"8134","DOI":"10.1039\/C4NR01268B","article-title":"The ultrastructure of type I collagen at nanoscale: Large or small D-spacing distribution?","volume":"6","author":"Su","year":"2014","journal-title":"Nanoscale"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0167-4838(96)00092-1","article-title":"Thermal stability of calf skin collagen type I in salt solutions","volume":"1297","author":"Koynova","year":"1996","journal-title":"BBA Protein Struct. Mol. Enzymol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1002\/bip.20742","article-title":"Temperature induced denaturation of collagen in acidic solution","volume":"86","author":"Mu","year":"2007","journal-title":"Biopolymers"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/0167-4838(84)90010-4","article-title":"A differential scanning calorimetry analysis of the age-related changes in the thermal stability of rat skin collagen","volume":"791","author":"Flandin","year":"1984","journal-title":"Biochim. Biophys. Acta."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1875","DOI":"10.1002\/bip.360251006","article-title":"Multiple denaturational transitions in fibrillar collagen","volume":"25","author":"Wallace","year":"1986","journal-title":"Biopolymers"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.tca.2012.08.024","article-title":"Revisit the pre-transition of type I collagen denaturation in dilute solution by ultrasensitive differential scanning calorimetry","volume":"548","author":"He","year":"2012","journal-title":"Thermochim. Acta"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"8147","DOI":"10.1021\/bi980360n","article-title":"Denaturation of type I collagen fibrils is an endothermic process accompanied by a noticeable change in the partial heat capacity","volume":"37","author":"Tiktopulo","year":"1998","journal-title":"Biochemistry"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1016\/j.jmb.2004.12.001","article-title":"The increase in denaturation temperature following cross-linking of collagen is caused by dehydration of the fibres","volume":"346","author":"Miles","year":"2005","journal-title":"J. Mol. Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"R28","DOI":"10.1111\/j.1365-2621.2005.tb09055.x","article-title":"Chemical reactions and stability of riboflavin in foods","volume":"70","author":"Choe","year":"2005","journal-title":"J. Food Sci."},{"key":"ref_39","unstructured":"Khalid, M.A.A. (2019). Application of riboflavin photochemical properties in hydrogel synthesis. Biophysical Chemistry\u2014Advance Applications, IntechOpen."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1006\/bbrc.1998.8936","article-title":"Detection of superoxide radicals and peroxynitrite by 1-hydroxy-4-phosphonooxy-2,2,6,6-tetramethylpiperidine: Quantification of extracellular superoxide radicals formation","volume":"248","author":"Dikalov","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1063\/1.555739","article-title":"Reactivity of HO2\/O2 radicals in aqueous solution","volume":"14","author":"Bielski","year":"1985","journal-title":"J. Phys. Chem. Ref. Data"},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Collin, F. (2019). Chemical basis of reactive oxygen species reactivity and involvement in neurodegenerative diseases. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20102407"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1793","DOI":"10.1515\/bchm2.1975.356.2.1793","article-title":"Isolation and characterization of pepsin-treated type III collagen from calf skin","volume":"356","author":"Fujii","year":"1975","journal-title":"Hoppe-Seyler\u2019s Z. Phys. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1172\/JCI108634","article-title":"Collagen polymorphism in normal and cirrhotic human liver","volume":"59","author":"Seyer","year":"1977","journal-title":"J. Clin. Investig."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"1498","DOI":"10.1172\/JCI108420","article-title":"Collagen polymorphism in idiopathic chronic pulmonary fibrosis","volume":"57","author":"Seyer","year":"1976","journal-title":"J. Clin. Investig."},{"key":"ref_46","first-page":"53","article-title":"Extraction, purification and physical characterization of collagen from body wall of sea cucumber Bohadschia bivitatta","volume":"4","author":"Siddiqui","year":"2013","journal-title":"Health Environ. J."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1016\/S2095-3119(17)61751-9","article-title":"The characterization of acid and pepsin soluble collagen from ovine bones (Ujumuqin sheep)","volume":"17","author":"Gao","year":"2018","journal-title":"J. Integr. Agric."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Blanco, M., V\u00e1zquez, J.A., P\u00e9rez-Mart\u00edn, R.I., and Sotelo, C.G. (2019). Collagen extraction optimization from the skin of the small-spotted catshark (S. canicula) by response surface methodology. Mar. Drugs, 17.","DOI":"10.3390\/md17010040"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"5687","DOI":"10.1007\/s12649-019-00843-2","article-title":"Collagen extraction from various waste bovine hide sources","volume":"11","author":"Noorzai","year":"2020","journal-title":"Waste Biomass Valori."},{"key":"ref_50","first-page":"481","article-title":"Collagen formation and structure","volume":"Volume 5","author":"Liu","year":"2010","journal-title":"Comprehensive Natural Products II. Chemistry and Biology, Aminoacids, Peptides and Proteins"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"5126","DOI":"10.1073\/pnas.83.14.5126","article-title":"In vitro regulation of cartilage matrix assembly by a Mr 54,000 collagen-binding proteins","volume":"83","author":"Chandrasekhar","year":"1986","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1242\/jcs.95.4.649","article-title":"Collagen fibrillogenesis in vitro: Interaction of types I and V collagen regulates fibril diameter","volume":"95","author":"Birk","year":"1990","journal-title":"J. Cell Sci."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1643","DOI":"10.1016\/j.msec.2009.01.001","article-title":"pH effects on collagen fibrillogenesis in vitro: Electrostatic interactions and phosphate binding","volume":"29","author":"Li","year":"2009","journal-title":"Mater. Sci. Eng. C"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"2801","DOI":"10.1039\/c4nj00123k","article-title":"The influence of hydroxypropyl \u03b2-cyclodextrin on the micellar to gel transition in F127 solutions investigated at macro and nanoscale levels","volume":"38","author":"Micutz","year":"2014","journal-title":"New J. Chem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"4258","DOI":"10.1021\/acs.jpcb.6b02199","article-title":"Interaction between albumin and Pluronic F127 block copolymer by global and local physicochemical profiling","volume":"120","author":"Neacsu","year":"2016","journal-title":"J. Phys. Chem. B"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/j.molliq.2018.01.162","article-title":"Influence of hydrocarbon moieties of partially fluorinated N-benzoyl thiourea compounds on their gelation properties. A detailed rheological study of complex viscoelastic behavior of decanol\/N-benzoyl thiourea mixtures","volume":"255","author":"Staicu","year":"2018","journal-title":"J. Mol. Liq."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"38391","DOI":"10.1039\/C5RA02708J","article-title":"Analysis of bimodal thermally-induced denaturation of type I collagen extracted from calfskin","volume":"5","author":"Staicu","year":"2015","journal-title":"RSC Adv."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1006\/jmrb.1994.1062","article-title":"Simulation of multiple isotropic spin-trap EPR spectra","volume":"104","author":"Duling","year":"1994","journal-title":"J. Magn. Reson. B"},{"key":"ref_59","unstructured":"Duling, D.R. (1996). PEST Winsim, National Institute of Environmental Health Sciences. Version 0.96;."},{"key":"ref_60","unstructured":"Mayne, R., and Burgeson, R.E. (1987). The classical collagens: Types I, II, and III. Structure and Function of Collagen Types, Academic Press."},{"key":"ref_61","unstructured":"Ventre, M., Padovani, M., Covington, A.D., and Netti, P.A. (2006, January 24\u201327). Composition, structure and physical properties of foetal calf skin. Proceedings of the II IULTCS Eurocongress: Innovation and New Technologies for the Future of Global Leather Industry, Istanbul, Turkey."}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/27\/1\/190\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T07:55:18Z","timestamp":1760169318000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/27\/1\/190"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,12,29]]},"references-count":61,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2022,1]]}},"alternative-id":["molecules27010190"],"URL":"https:\/\/doi.org\/10.3390\/molecules27010190","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,12,29]]}}}