{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T11:13:04Z","timestamp":1792753984127,"version":"4.5.0"},"reference-count":62,"publisher":"MDPI AG","issue":"21","license":[{"start":{"date-parts":[[2021,11,2]],"date-time":"2021-11-02T00:00:00Z","timestamp":1635811200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Lysozyme is often used as a model protein to study interaction with drug molecules and to understand biological processes which help in illuminating the therapeutic effectiveness of the drug. In the present work, in vitro interaction studies of 1-{(2-hydroxyethyl)amino}-2-amino-1,2-dideoxy-d-glucose triphenyl tin (IV) (GATPT) complex with lysozyme were carried out by employing various biophysical methods such as absorption, fluorescence, and circular dichroism (CD) spectroscopies. The experimental results revealed efficient binding affinity of GATPT with lysozyme with intrinsic binding (Kb) and binding constant (K) values in the order of 105 M\u22121. The number of binding sites and thermodynamic parameters \u0394G, \u0394H, and \u0394S at four different temperatures were also calculated and the interaction of GATPT with lysozyme was found to be enthalpy and entropy driven. The CD spectra revealed alterations in the population of \u03b1\u2013helical content within the secondary structure of lysozyme in presence of GATPT complex. The morphological analysis of the complex with lysozyme and lysozyme-DNA condensates was carried out by employing confocal and SEM studies. Furthermore, the molecular docking studies confirmed the interaction of GATPT within the larger hydrophobic pocket of the lysozyme via several non-covalent interactions.<\/jats:p>","DOI":"10.3390\/molecules26216641","type":"journal-article","created":{"date-parts":[[2021,11,2]],"date-time":"2021-11-02T22:17:23Z","timestamp":1635891443000},"page":"6641","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Interaction of Carrier Protein with Potential Metallic Drug Candidate N-Glycoside \u2018GATPT\u2019: Validation by Multi-Spectroscopic and Molecular Docking Approaches"],"prefix":"10.3390","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3953-3248","authenticated-orcid":false,"given":"Sabiha","family":"Parveen","sequence":"first","affiliation":[{"name":"Department of Chemistry, Aligarh Muslim University, Aligarh 202002, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohd. Sajid","family":"Ali","sequence":"additional","affiliation":[{"name":"Department of Chemistry, College of Sciences, King Saud University, Riyadh 11451, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hamad A.","family":"Al-Lohedan","sequence":"additional","affiliation":[{"name":"Department of Chemistry, College of Sciences, King Saud University, Riyadh 11451, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5301-898X","authenticated-orcid":false,"given":"Sartaj","family":"Tabassum","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Aligarh Muslim University, Aligarh 202002, India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,11,2]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"5526","DOI":"10.1016\/j.bbagen.2013.04.023","article-title":"Albumin as a versatile platform for drug half-life extension","volume":"1830","author":"Sleep","year":"2013","journal-title":"Biochim. 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