{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T15:54:53Z","timestamp":1787068493477,"version":"build-2736575974"},"reference-count":29,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2018,7,31]],"date-time":"2018-07-31T00:00:00Z","timestamp":1532995200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100010663","name":"H2020 European Research Council","doi-asserted-by":"publisher","award":["GINOP-2.3.2-15-2016-00049"],"award-info":[{"award-number":["GINOP-2.3.2-15-2016-00049"]}],"id":[{"id":"10.13039\/100010663","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Tilmicosin is a widely used antibiotic in veterinary applications. Its antimicrobial activity is ranged from Gram-positive and some Gram-negative bacteria towards activities against Mycoplasma and Chlamydia. Adsorption affinity of tilmicosin antibiotics towards bovine serum albumin was investigated by both spectroscopic (UV-vis, Photoluminescence) and calorimetric methods. The interaction was determined on the basis of quenching of albumin by tilmicosin. Results confirm noncovalent binding of tilmicosin on bovine serum albumin with 1:1 stoichiometry associated with pK = 4.5, highlighting possible removal of tilmicosin molecules from the albumin surface through exchange reactions by known competitor molecules. Calorimetric measurements have confirmed the weak interaction between tilmicosin and albumin and reflect enhanced denaturation of the albumin in the presence of tilmicosin antibiotic. This process is associated with the decreased activation energy of conformational transition of the albumin. It opens a new, very quick reaction pathway without any significant effect on the product by noncovalent binding the tilmicosin molecules to the protein molecules. Results highlight the medical importance of these investigations by considerable docking of the selected antibiotic molecules on serum albumins. Although the binding may cause toxic effects in living bodies, the strength of the binding is weak enough to find competitor molecules for effective removals from their surface.<\/jats:p>","DOI":"10.3390\/molecules23081915","type":"journal-article","created":{"date-parts":[[2018,8,1]],"date-time":"2018-08-01T03:10:01Z","timestamp":1533093001000},"page":"1915","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Noncovalent Interaction of Tilmicosin with Bovine Serum Albumin"],"prefix":"10.3390","volume":"23","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8903-1337","authenticated-orcid":false,"given":"Be\u00e1ta","family":"Lemli","sequence":"first","affiliation":[{"name":"Department of Pharmaceutical Chemistry, Faculty of Pharmacy, University of P\u00e9cs, R\u00f3kus 2, H-7624 P\u00e9cs, Hungary"},{"name":"Department of General and Physical Chemistry, University of P\u00e9cs, Ifj\u00fas\u00e1g 6, H-7624 P\u00e9cs, Hungary"},{"name":"J\u00e1nos Szent\u00e1gothai Research Center, Ifj\u00fas\u00e1g 20, H-7624 P\u00e9cs, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Di\u00e1na","family":"Derd\u00e1k","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Chemistry, Faculty of Pharmacy, University of P\u00e9cs, R\u00f3kus 2, H-7624 P\u00e9cs, Hungary"},{"name":"Department of General and Physical Chemistry, University of P\u00e9cs, Ifj\u00fas\u00e1g 6, H-7624 P\u00e9cs, Hungary"},{"name":"J\u00e1nos Szent\u00e1gothai Research Center, Ifj\u00fas\u00e1g 20, H-7624 P\u00e9cs, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P\u00e9ter","family":"Laczay","sequence":"additional","affiliation":[{"name":"Department of Food Hygiene, University of Veterinary Medicine, Istv\u00e1n 2, H-1078 Budapest, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dorottya","family":"Kov\u00e1cs","sequence":"additional","affiliation":[{"name":"Department of General and Physical Chemistry, University of P\u00e9cs, Ifj\u00fas\u00e1g 6, H-7624 P\u00e9cs, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S\u00e1ndor","family":"Kuns\u00e1gi-M\u00e1t\u00e9","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Chemistry, Faculty of Pharmacy, University of P\u00e9cs, R\u00f3kus 2, H-7624 P\u00e9cs, Hungary"},{"name":"Department of General and Physical Chemistry, University of P\u00e9cs, Ifj\u00fas\u00e1g 6, H-7624 P\u00e9cs, Hungary"},{"name":"J\u00e1nos Szent\u00e1gothai Research Center, Ifj\u00fas\u00e1g 20, H-7624 P\u00e9cs, Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2018,7,31]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1039\/an9941902577","article-title":"Determination of tilmicosin in ovine milk using high-performance liquid chromatography","volume":"119","author":"Parker","year":"1994","journal-title":"Analyst"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1021\/jf2037449","article-title":"Development and validation of an indirect competitive enzyme-linked immunosorbent assay for the screening of tylosin and tilmicosin in muscle, liver, milk, honey and eggs","volume":"60","author":"Peng","year":"2012","journal-title":"J. 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