{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T19:57:29Z","timestamp":1785182249914,"version":"3.55.0"},"reference-count":46,"publisher":"MDPI AG","issue":"13","license":[{"start":{"date-parts":[[2025,6,25]],"date-time":"2025-06-25T00:00:00Z","timestamp":1750809600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Alberta Innovates Concepts Grant"},{"name":"Strategic Research Program"},{"name":"Alberta Innovates Alliance Grant"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Understanding the binding interactions between protein-bound uremic toxins (PBUTs) and human serum albumin (HSA) is critical for advancing treatments for chronic kidney disease (CKD). While previous studies have suggested that putrescine, a diamine PBUT, exhibits moderate binding affinity to HSA, this study provides evidence of the contrary. Using isothermal titration calorimetry and saturation transfer difference nuclear magnetic resonance , we demonstrate that putrescine\u2019s interaction with HSA is weak, non-specific, and thermodynamically negligible in the range of conditions studied. Unlike earlier studies relying on spectroscopy techniques such as UV\u2013visible absorption and fluorescence, which may overestimate binding strength, the results presented here highlight the limitations of indirect methodologies and underscore the importance of more sensitive approaches for accurate energy characterization. Our findings suggest that putrescine only weakly interacts non-specifically with HSA and may bind more preferentially to other plasma proteins, contributing to its accumulation in CKD patients.<\/jats:p>","DOI":"10.3390\/ijms26136084","type":"journal-article","created":{"date-parts":[[2025,6,25]],"date-time":"2025-06-25T03:53:02Z","timestamp":1750823582000},"page":"6084","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Human Serum Albumin Affinity for Putrescine Using ITC and STD-NMR"],"prefix":"10.3390","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-9677-7312","authenticated-orcid":false,"given":"Vida","family":"Dehghan Niestanak","sequence":"first","affiliation":[{"name":"Department of Biomedical Engineering, University of Alberta, Edmonton, AB T6G 2V4, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0255-159X","authenticated-orcid":false,"given":"Ryan","family":"McKay","sequence":"additional","affiliation":[{"name":"Department of Chemistry, University of Alberta, Edmonton, AB T6G 2V4, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marcello","family":"Tonelli","sequence":"additional","affiliation":[{"name":"Department of Medicine, University of Calgary, Calgary, AB T2N 2T8, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3162-3545","authenticated-orcid":false,"given":"Larry D.","family":"Unsworth","sequence":"additional","affiliation":[{"name":"Department of Biomedical Engineering, University of Alberta, Edmonton, AB T6G 2V4, Canada"},{"name":"Department of Chemical and Materials Engineering, University of Alberta, Edmonton, AB T6G 2V4, Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,6,25]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Holmar, J., de la Puente-Secades, S., Floege, J., Noels, H., Jankowski, J., and Orth-Alampour, S. 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