{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,25]],"date-time":"2026-01-25T15:06:36Z","timestamp":1769353596879,"version":"3.49.0"},"reference-count":35,"publisher":"Georg Thieme Verlag KG","issue":"12","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Drug Res (Stuttg)"],"published-print":{"date-parts":[[2020,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>This current research aimed to establish the most required pharmacodynamics parameters of two transition metal complexes of an antimicrobial drug secnidazole. The spectroscopic fluorescence quenching strategy was outlined to evaluate the binding mechanism and binding affinity of nickel (II) and chromium (III) complexes of secnidazole with bovine serum albumin (BSA). The conformational modifications and the interacting patterns of the protein due to the interaction of the parent compound of the metal complexes have been investigated by molecular docking approach. The ligand-protein interactions were confirmed by the spectral quelling of the serum protein\u2019s intensity in the presence of metal chelate of secnidazole. The quenching mechanism was an endothermic dynamic process. The calculated thermodynamic factors delineated van der Waals interactions mainly influenced the spontaneous process. The UV-fluorescence curves were studied to establish the energy transformation profile according to the F\u00f6rster resonance energy transfer (FRET) theory. The double-logarithm plot exhibited the binding number that ensured the drug-protein interaction was at a 1:1 ratio. The compared binding constants dictated that both metal chelates gained higher binding affinity, longer half-life, and achieved the capacity to show the pharmacological effects by a lower dose than the parent molecule.<\/jats:p>","DOI":"10.1055\/a-1252-2322","type":"journal-article","created":{"date-parts":[[2020,10,23]],"date-time":"2020-10-23T23:01:57Z","timestamp":1603494117000},"page":"583-592","source":"Crossref","is-referenced-by-count":8,"title":["Transition Metal Chelation Augments the Half-life of Secnidazole: Molecular Docking and Fluorescence Spectroscopic Approaches"],"prefix":"10.1055","volume":"70","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9706-207X","authenticated-orcid":false,"given":"Md. Jamal","family":"Hossain","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Chemistry, Faculty of Pharmacy, University of Dhaka, Dhaka-1000, Bangladesh"},{"name":"Department of Pharmaceutical Chemistry, Faculty of Pharmacy, University of Dhaka, Dhaka-1000, Bangladesh"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mohammad A.","family":"Rashid","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Chemistry, Faculty of Pharmacy, University of Dhaka, Dhaka-1000, Bangladesh"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Md. Zakir","family":"Sultan","sequence":"additional","affiliation":[{"name":"Centre for Advanced Research in Sciences (CARS), University of Dhaka, Dhaka-1000, Bangladesh"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"194","published-online":{"date-parts":[[2020,10,23]]},"reference":[{"key":"ref1","first-page":"2299","article-title":"Antimicrobial effects of silver (I) and bismuth (III) complexes with secnidazole-derived schiff base ligands: The role of the nitro group reduction","volume":"30","author":"AP A Oliveira","year":"2019","journal-title":"J Braz Chem Soc"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"121","DOI":"10.21010\/ajtcam.v13i6.17","article-title":"Studies on the interaction between triptolide and bovine serum albumin (BSA) by spectroscopic and molecular modeling methods","volume":"13","author":"H Wang","year":"2016","journal-title":"Afr J Tradit Complement Altern Med"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.saa.2013.06.007","article-title":"Spectroscopic studies on the interaction between tetrandrine and two serum albumins by chemometrics methods","volume":"115","author":"Z Cheng","year":"2013","journal-title":"Spectrochim Acta A Mol Biomol Spectrosc"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1016\/j.saa.2013.11.016","article-title":"Molecular modeling and spectroscopic studies on the interaction of the chiral drug venlafaxine hydrochloride with bovine serum albumin","volume":"122","author":"N Shahabadi","year":"2014","journal-title":"Spectrochim Acta A Mol Biomol Spectrosc"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.ijbiomac.2006.03.020","article-title":"Studies on the interaction between oxaprozin-E and bovine serum albumin by spectroscopic methods","volume":"39","author":"S F Sun","year":"2006","journal-title":"Int J Biol Macromol"},{"key":"ref6","doi-asserted-by":"publisher","first-page":"e01631","DOI":"10.1016\/j.heliyon.2019.e01631","article-title":"Antidepressant drug-protein interactions studied by spectroscopic methods based on fluorescent carbon quantum dots","volume":"5","author":"SK Vaishanav Reshma","year":"2019","journal-title":"Heliyon"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1007\/s10895-007-0226-9","article-title":"Study on the interaction between florasulam and bovine serum albumin","volume":"17","author":"D Ran","year":"2007","journal-title":"J Fluoresc"},{"key":"ref8","first-page":"21","article-title":"Fluorescence spectroscopic studies of in vitro interactions of famotidine and tapentadol hydrochloride with bovine serum albumin. 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