{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T16:32:25Z","timestamp":1790181145461,"version":"4.1.0"},"reference-count":76,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2023,9,8]],"date-time":"2023-09-08T00:00:00Z","timestamp":1694131200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Medical University of Bialystok, Poland","award":["B.SUB.23.250"],"award-info":[{"award-number":["B.SUB.23.250"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pharmaceuticals"],"abstract":"<jats:p>Background: Histamine H2 receptor antagonists are a group of drugs that inhibit gastric juice secretion in gastrointestinal diseases. However, there is evidence to suggest that H2 blockers have a broader spectrum of activity. The antioxidant properties of H2 blockers have not been fully elucidated, and their anti-glycation potential has not been studied to date. Therefore, this is the first study to compare the antioxidant and antiglycation potentials of the most popular H2 antagonists (ranitidine, cimetidine, and famotidine) on protein glycoxidation in vitro. Methods: Bovine serum albumin (BSA) was glycated using sugars (glucose, fructose, galactose, and ribose) as well as aldehydes (glyoxal and methylglyoxal). Results: In the analyzed group of drugs, ranitidine was the only H2 blocker that significantly inhibited BSA glycation in all tested models. The contents of protein carbonyls, protein glycoxidation products (\u2193dityrosine, \u2193N-formylkynurenine), and early (\u2193Amadori products) and late-stage (\u2193AGEs) protein glycation products decreased in samples of glycated BSA with the addition of ranitidine relative to BSA with the addition of the glycating agents. The anti-glycation potential of ranitidine was comparable to those of aminoguanidine and Trolox. In the molecular docking analysis, ranitidine was characterized by the lowest binding energy for BSA sites and could compete with protein amino groups for the addition of carbonyl groups. H2 blockers also scavenge free radicals. The strongest antioxidant properties are found in ranitidine, which additionally has the ability to bind transition metal ions. The systematic literature review also revealed that the anti-glycation effects of ranitidine could be attributed to its antioxidant properties. Conclusions: Ranitidine showed anti-glycation and antioxidant properties. Further research is needed, particularly in patients with diseases that promote protein glycation.<\/jats:p>","DOI":"10.3390\/ph16091273","type":"journal-article","created":{"date-parts":[[2023,9,8]],"date-time":"2023-09-08T07:52:11Z","timestamp":1694159531000},"page":"1273","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Antioxidant and Anti-Glycation Potential of H2 Receptor Antagonists\u2014In Vitro Studies and a Systematic Literature Review"],"prefix":"10.3390","volume":"16","author":[{"given":"Grzegorz","family":"Biedrzycki","sequence":"first","affiliation":[{"name":"Hospital Pharmacy, Provincial Specialist Hospital in Olsztyn, 10-900 Olsztyn, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4724-4689","authenticated-orcid":false,"given":"Blanka","family":"Wolszczak-Biedrzycka","sequence":"additional","affiliation":[{"name":"Department of Psychology and Sociology of Health and Public Health, University of Warmia and Mazury in Olsztyn, 10-900 Olsztyn, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2391-3307","authenticated-orcid":false,"given":"Justyna","family":"Dorf","sequence":"additional","affiliation":[{"name":"Department of Clinical Laboratory Diagnostics, Medical University of Bialystok, 15-089 Bialystok, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0000-4056-2014","authenticated-orcid":false,"given":"Daniel","family":"Michalak","sequence":"additional","affiliation":[{"name":"Students Scientific Club \u201cBiochemistry of Civilization Diseases\u201d, Department of Hygiene, Epidemiology and Ergonomics, Medical University of Bialystok, 15-089 Bialystok, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4350-0369","authenticated-orcid":false,"given":"Ma\u0142gorzata","family":"\u017bendzian-Piotrowska","sequence":"additional","affiliation":[{"name":"Department of Hygiene, Epidemiology and Ergonomics, Medical University of Bialystok, 15-089 Bialystok, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna","family":"Zalewska","sequence":"additional","affiliation":[{"name":"Experimental Dentistry Laboratory, Medical University of Bialystok, 15-089 Bialystok, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5609-3187","authenticated-orcid":false,"given":"Mateusz","family":"Maciejczyk","sequence":"additional","affiliation":[{"name":"Department of Hygiene, Epidemiology and Ergonomics, Medical University of Bialystok, 15-089 Bialystok, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,9,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Bertino, L., Guarneri, F., Cannav\u00f2, S.P., Casciaro, M., Pioggia, G., and Gangemi, S. 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