{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,12]],"date-time":"2025-10-12T03:52:51Z","timestamp":1760241171814,"version":"build-2065373602"},"reference-count":63,"publisher":"MDPI AG","issue":"24","license":[{"start":{"date-parts":[[2019,12,12]],"date-time":"2019-12-12T00:00:00Z","timestamp":1576108800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"French-Bulgarian RILA programme of the","award":["38675 VG"],"award-info":[{"award-number":["38675 VG"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Gold(III) porphyrin presents an attractive alternative to the use of, for example, cisplatin in chemotherapy. However, approaches that allow to selectively target cancer cells are highly sought. Many plant and mammalian lectins have been shown to bind oligosaccharide sequences of the aberrant glycosylation pattern found on cancerous tumors. For example human galectin-3, of the galectin family specific for \u03b2-galactoside, is overexpressed in the extracellular matrix of tumorigenous and metastatic tissues. We searched for non-carbohydrate ligands for galectin-3 that can guide a cytotoxic drug to the cancer cells by maintaining its affinity for tumor associated carbohydrate antigens. Previous findings showed that zinc tetrasulfonatophenylporphyrin can bind galectin-3 with sub-micromolar affinity without disturbing lactose binding. Gold(III) porphyrin is not only cytotoxic to cancer cells, it knows also a potential application as photosensitiser in photodynamic therapy. We investigated the binding of gold(III) porphyrin to galectin-3 using different biophysical interaction techniques and demonstrated a low micromolar affinity of human galectin-3 for the cytotoxic compound. Co-crystallization attempts in order to understand the binding mode of gold porphyrin to galectin-3 failed, but molecular docking emphasized a highly populated secondary binding site that does not hinder lactose or Thomsen Friendenreich disaccharide binding. This suggests that gold(III) porphyrin might significantly enhance its concentration and delivery to cancer cells by binding to human galectin-3 that keeps its orientation towards tumor associated carbohydrate antigens.<\/jats:p>","DOI":"10.3390\/molecules24244561","type":"journal-article","created":{"date-parts":[[2019,12,12]],"date-time":"2019-12-12T11:06:41Z","timestamp":1576148801000},"page":"4561","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["Binding of Gold(III) Porphyrin by the Pro-metastatic Regulatory Protein Human Galectin-3"],"prefix":"10.3390","volume":"24","author":[{"given":"Vanya","family":"Bogoeva","sequence":"first","affiliation":[{"name":"Institute of Molecular Biology \u201cRoumen Tsanev\u201c-Bulgarian Academy of Sciences (IMB-BAS), George Bonchev Street, bl. 21, 1113 Sofia, Bulgaria"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Miroslav","family":"Rangelov","sequence":"additional","affiliation":[{"name":"Institute of Organic Chemistry with Center for Phytochemistry-Bulgarian Academy of Sciences (IOCCP-BAS), George Bonchev Street, bl. 21, 1113 Sofia, Bulgaria"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nadezhda","family":"Todorova","sequence":"additional","affiliation":[{"name":"Institute of Biodiversity and Ecosystem Research-Bulgarian Academy of Sciences (IBER-BAS), 2 Yuri Gagarin Street, 1113 Sofia, Bulgaria"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Annie","family":"Lambert","sequence":"additional","affiliation":[{"name":"University of Nantes, CNRS, Unit for Functional and Engineered Proteins (UFIP), UMR 6286, F-44000 Nantes, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Clarisse","family":"Bridot","sequence":"additional","affiliation":[{"name":"Unit for Structural et Functional Glycobiologie (UGSF), UMR 8576 of the University of Lille and CNRS, 50 Av. De Halley, 59658 Villeneuve d\u2019Ascq, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anna","family":"Yordanova","sequence":"additional","affiliation":[{"name":"Institute of Molecular Biology \u201cRoumen Tsanev\u201c-Bulgarian Academy of Sciences (IMB-BAS), George Bonchev Street, bl. 21, 1113 Sofia, Bulgaria"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Goedele","family":"Roos","sequence":"additional","affiliation":[{"name":"Unit for Structural et Functional Glycobiologie (UGSF), UMR 8576 of the University of Lille and CNRS, 50 Av. De Halley, 59658 Villeneuve d\u2019Ascq, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9775-6917","authenticated-orcid":false,"given":"Cyrille","family":"Grandjean","sequence":"additional","affiliation":[{"name":"University of Nantes, CNRS, Unit for Functional and Engineered Proteins (UFIP), UMR 6286, F-44000 Nantes, France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8112-1442","authenticated-orcid":false,"given":"Julie","family":"Bouckaert","sequence":"additional","affiliation":[{"name":"Unit for Structural et Functional Glycobiologie (UGSF), UMR 8576 of the University of Lille and CNRS, 50 Av. De Halley, 59658 Villeneuve d\u2019Ascq, France"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2019,12,12]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"20807","DOI":"10.1016\/S0021-9258(17)31891-4","article-title":"Galectins. Structure and function of a large family of animal lectins","volume":"269","author":"Barondes","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Johannes, L., Jacob, R., and Leffler, H. (2018). Galectins at a glance. J. Cell. Sc.i, 131.","DOI":"10.1242\/jcs.208884"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/S0304-4165(99)00177-4","article-title":"Secretion of the galectin family of mammalian carbohydrate-binding proteins","volume":"1473","author":"Hughes","year":"1999","journal-title":"Biochim. Biophys. 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