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The amount of hydrogen sulfide (H2S) is known to be significantly reduced in the brain tissue of people diagnosed with Alzheimer\u2019s disease relative to that of healthy individuals. These findings prompted us to investigate the effects of H2S on the formation of amyloids in vitro using a model fibrillogenic protein hen egg white lysozyme (HEWL). HEWL forms typical \u03b2-sheet rich fibrils during the course of 70 min at low pH and high temperatures. The addition of H2S completely inhibits the formation of \u03b2-sheet and amyloid fibrils, as revealed by deep UV resonance Raman (DUVRR) spectroscopy and ThT fluorescence. Nonresonance Raman spectroscopy shows that disulfide bonds undergo significant rearrangements in the presence of H2S. Raman bands corresponding to disulfide (RSSR) vibrational modes in the 550\u2013500 cm\u20131 spectral range decrease in intensity and are accompanied by the appearance of a new 490 cm\u20131 band assigned to the trisulfide group (RSSSR) based on the comparison with model compounds. The formation of RSSSR was proven further using a reaction with TCEP reduction agent and LC-MS analysis of the products. Intrinsic tryptophan fluorescence study shows a strong denaturation of HEWL containing trisulfide bonds. The presented evidence indicates that H2S causes the formation of trisulfide bridges, which destabilizes HEWL structure, preventing protein fibrillation. As a result, small spherical aggregates of unordered protein form, which exhibit no cytotoxicity by contrast with HEWL fibrils.<\/jats:p>","DOI":"10.1021\/jp508471v","type":"journal-article","created":{"date-parts":[[2014,12,29]],"date-time":"2014-12-29T12:54:05Z","timestamp":1419857645000},"page":"1265-1274","source":"Crossref","is-referenced-by-count":42,"title":["Hydrogen Sulfide Inhibits Amyloid Formation"],"prefix":"10.1021","volume":"119","author":[{"given":"Manuel F.","family":"Rosario-Alomar","sequence":"first","affiliation":[{"name":"University of Puerto Rico at Mayagu\u0308ez , , ,","place":["Mayagu\u0308ez, Puerto Rico, 00693"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tatiana","family":"Quin\u0303ones-Ruiz","sequence":"additional","affiliation":[{"name":"University at Albany, SUNY , , , ,","place":["Albany, New York, United States, 12222"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dmitry","family":"Kurouski","sequence":"additional","affiliation":[{"name":"University at Albany, SUNY , , , ,","place":["Albany, New York, United States, 12222"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Valentin","family":"Sereda","sequence":"additional","affiliation":[{"name":"University at Albany, SUNY , , , ,","place":["Albany, New York, United States, 12222"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eduardo B.","family":"Ferreira","sequence":"additional","affiliation":[{"name":"University at Albany, SUNY , , , ,","place":["Albany, New York, United States, 12222"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lorraine De","family":"Jesu\u0301s-Kim","sequence":"additional","affiliation":[{"name":"University of Puerto Rico at Mayagu\u0308ez , , ,","place":["Mayagu\u0308ez, Puerto Rico, 00693"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Samuel","family":"Herna\u0301ndez-Rivera","sequence":"additional","affiliation":[{"name":"University of Puerto Rico at Mayagu\u0308ez , , ,","place":["Mayagu\u0308ez, Puerto Rico, 00693"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dmitri V.","family":"Zagorevski","sequence":"additional","affiliation":[{"name":"Rensselaer Polytechnic Institute , , , ,","place":["Troy, New York, United States, 12180"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Juan","family":"Lo\u0301pez-Garriga","sequence":"additional","affiliation":[{"name":"University of Puerto Rico at Mayagu\u0308ez , , ,","place":["Mayagu\u0308ez, Puerto Rico, 00693"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Igor K.","family":"Lednev","sequence":"additional","affiliation":[{"name":"University at Albany, SUNY , , , ,","place":["Albany, New York, United States, 12222"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2014,12,29]]},"reference":[{"key":"2026090219013582500_cit1","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/S0925-4439(00)00029-6","article-title":"Alzheimer\u2019s\namyloid fibrils: structure and assembly","volume":"1502","author":"Serpell","year":"2000","journal-title":"Biochim.\nBiophys. Acta, Mol. Basis Dis."},{"key":"2026090219013582500_cit2","doi-asserted-by":"crossref","first-page":"2552","DOI":"10.1021\/bi991447r","article-title":"Fibrils formed\nin vitro from alpha-synuclein and two mutant forms linked to Parkinson\u2019s\ndisease are typical amyloid","volume":"39","author":"Conway","year":"2000","journal-title":"Biochemistry"},{"key":"2026090219013582500_cit3","first-page":"1","article-title":"Aggregation-prone\nproteins modulate\nhuntingtin inclusion body formation in yeast","volume":"6","author":"Kantcheva","year":"2014","journal-title":"PLoS Curr. Huntington\u2019s Dis."},{"key":"2026090219013582500_cit4","doi-asserted-by":"crossref","first-page":"1283","DOI":"10.1056\/NEJM198006053022305","article-title":"Amyloid\ndeposits and amyloidosis. The beta-fibrilloses (first of two parts)","volume":"302","author":"Glenner","year":"1980","journal-title":"N. Engl. J. Med."},{"key":"2026090219013582500_cit5","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1016\/S0969-2126(96)00104-9","article-title":"Synchrotron X-ray studies suggest that the core of\nthe transthyretin amyloid fibril is a continuous beta-sheet helix","volume":"4","author":"Blake","year":"1996","journal-title":"Structure"},{"key":"2026090219013582500_cit6","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1016\/j.bpj.2014.02.007","article-title":"Amyloid\nfibrils: the eighth wonder of the world in protein folding and aggregation","volume":"106","author":"Lednev","year":"2014","journal-title":"Biophys. J."},{"key":"2026090219013582500_cit7","doi-asserted-by":"crossref","first-page":"10737","DOI":"10.1074\/jbc.M010907200","article-title":"Evidence for a partially folded intermediate in alpha-synuclein\nfibril formation","volume":"276","author":"Uversky","year":"2001","journal-title":"J. Biol. 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Phys."},{"key":"2026090219013582500_cit25","doi-asserted-by":"crossref","first-page":"1154","DOI":"10.1021\/bc4000299","article-title":"Trisulfide\nmodification impacts the reduction step in antibody\u2013drug conjugation\nprocess","volume":"24","author":"Cumnock","year":"2013","journal-title":"Bioconjugate Chem."},{"key":"2026090219013582500_cit26","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1002\/jbio.200710013","article-title":"Hen egg\nwhite lysozyme\nfibrillation: a deep-UV resonance Raman spectroscopic study","volume":"1","author":"Xu","year":"2008","journal-title":"J. Biophotonics"},{"key":"2026090219013582500_cit27","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/0022-1759(83)90303-4","article-title":"Rapid colorimetric\nassay for cellular growth and survival: Application to proliferation\nand cytotoxicity assays","volume":"65","author":"Mosmann","year":"1983","journal-title":"J. Immunol. Methods"},{"key":"2026090219013582500_cit28","doi-asserted-by":"crossref","first-page":"4960","DOI":"10.1021\/bi00339a035","article-title":"Ultraviolet resonance\nRaman spectra of cytochrome c\nconformational states","volume":"24","author":"Copeland","year":"1985","journal-title":"Biochemistry"},{"key":"2026090219013582500_cit29","doi-asserted-by":"crossref","first-page":"4271","DOI":"10.1021\/jp065247i","article-title":"Peptide bond vibrational\ncoupling","volume":"111","author":"Myshakina","year":"2007","journal-title":"J. Phys. Chem. B"},{"key":"2026090219013582500_cit30","doi-asserted-by":"crossref","first-page":"6359","DOI":"10.1021\/ja00017a002","article-title":"UVRR spectroscopy\nof the peptide bond. 1. Amide S, a nonhelical structure marker, is\na C.alpha.H bending mode","volume":"113","author":"Wang","year":"1991","journal-title":"J. Am. Chem. Soc."},{"key":"2026090219013582500_cit31","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1002\/bip.20330","article-title":"Lysozyme fibrillation:\nDeep UV Raman spectroscopic\ncharacterization of protein structural transformation","volume":"79","author":"Xu","year":"2005","journal-title":"Biopolymers"},{"key":"2026090219013582500_cit32","doi-asserted-by":"crossref","first-page":"11002","DOI":"10.1021\/ja073798w","article-title":"Probing the cross-\u03b2 core structure\nof amyloid fibrils by hydrogen\u2013deuterium exchange deep ultraviolet\nresonance Raman spectroscopy","volume":"129","author":"Xu","year":"2007","journal-title":"J. Am. Chem. Soc."},{"key":"2026090219013582500_cit33","article-title":"Vibrational\nspectroscopy: Biological applications of ultraviolet Raman spectroscopy","volume-title":"Protein Structures, Methods in Protein Structures and\nStability Analysis","author":"Lednev","year":"2007"},{"key":"2026090219013582500_cit34","doi-asserted-by":"crossref","first-page":"11775","DOI":"10.1021\/ja0039738","article-title":"Dihedral \u03c8\nangle dependence\nof the amide III vibration: A uniquely sensitive UV resonance Raman\nsecondary structural probe","volume":"123","author":"Asher","year":"2001","journal-title":"J. Am. Chem. 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Nanotechnol."},{"key":"2026090219013582500_cit44","doi-asserted-by":"crossref","first-page":"2648","DOI":"10.1021\/jo00008a014","article-title":"Selective\nreduction of disulfides by tris(2-carboxyethyl)phosphine","volume":"56","author":"Burns","year":"1991","journal-title":"J. Org. Chem."},{"key":"2026090219013582500_cit45","doi-asserted-by":"crossref","first-page":"6045","DOI":"10.1021\/ja00386a034","article-title":"Sulfur-sulfur bond cleavage processes. Selective desulfurization\nof trisulfides","volume":"104","author":"Harpp","year":"1982","journal-title":"J. Am. Chem. Soc."},{"key":"2026090219013582500_cit46","doi-asserted-by":"crossref","first-page":"7048","DOI":"10.1002\/anie.201100986","article-title":"Disulfide\nbonds reduce the toxicity of the amyloid\nfibrils formed by an extracellular protein","volume":"50","author":"Mossuto","year":"2011","journal-title":"Angew. Chem., Int. 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