{"language":[{"iso":"eng"}],"publication":"Molecules","year":"2023","user_id":"48864","_id":"46542","status":"public","publisher":"MDPI AG","type":"journal_article","keyword":["Chemistry (miscellaneous)","Analytical Chemistry","Organic Chemistry","Physical and Theoretical Chemistry","Molecular Medicine","Drug Discovery","Pharmaceutical Science"],"article_number":"6060","citation":{"ama":"Huang J, Qiu Y, Lücke F, Su J, Grundmeier G, Keller A. Multiprotein Adsorption from Human Serum at Gold and Oxidized Iron Surfaces Studied by Atomic Force Microscopy and Polarization-Modulation Infrared Reflection Absorption Spectroscopy. <i>Molecules</i>. 2023;28(16). doi:<a href=\"https://doi.org/10.3390/molecules28166060\">10.3390/molecules28166060</a>","bibtex":"@article{Huang_Qiu_Lücke_Su_Grundmeier_Keller_2023, title={Multiprotein Adsorption from Human Serum at Gold and Oxidized Iron Surfaces Studied by Atomic Force Microscopy and Polarization-Modulation Infrared Reflection Absorption Spectroscopy}, volume={28}, DOI={<a href=\"https://doi.org/10.3390/molecules28166060\">10.3390/molecules28166060</a>}, number={166060}, journal={Molecules}, publisher={MDPI AG}, author={Huang, Jingyuan and Qiu, Yunshu and Lücke, Felix and Su, Jiangling and Grundmeier, Guido and Keller, Adrian}, year={2023} }","ieee":"J. Huang, Y. Qiu, F. Lücke, J. Su, G. Grundmeier, and A. Keller, “Multiprotein Adsorption from Human Serum at Gold and Oxidized Iron Surfaces Studied by Atomic Force Microscopy and Polarization-Modulation Infrared Reflection Absorption Spectroscopy,” <i>Molecules</i>, vol. 28, no. 16, Art. no. 6060, 2023, doi: <a href=\"https://doi.org/10.3390/molecules28166060\">10.3390/molecules28166060</a>.","short":"J. Huang, Y. Qiu, F. Lücke, J. Su, G. Grundmeier, A. Keller, Molecules 28 (2023).","apa":"Huang, J., Qiu, Y., Lücke, F., Su, J., Grundmeier, G., &#38; Keller, A. (2023). Multiprotein Adsorption from Human Serum at Gold and Oxidized Iron Surfaces Studied by Atomic Force Microscopy and Polarization-Modulation Infrared Reflection Absorption Spectroscopy. <i>Molecules</i>, <i>28</i>(16), Article 6060. <a href=\"https://doi.org/10.3390/molecules28166060\">https://doi.org/10.3390/molecules28166060</a>","mla":"Huang, Jingyuan, et al. “Multiprotein Adsorption from Human Serum at Gold and Oxidized Iron Surfaces Studied by Atomic Force Microscopy and Polarization-Modulation Infrared Reflection Absorption Spectroscopy.” <i>Molecules</i>, vol. 28, no. 16, 6060, MDPI AG, 2023, doi:<a href=\"https://doi.org/10.3390/molecules28166060\">10.3390/molecules28166060</a>.","chicago":"Huang, Jingyuan, Yunshu Qiu, Felix Lücke, Jiangling Su, Guido Grundmeier, and Adrian Keller. “Multiprotein Adsorption from Human Serum at Gold and Oxidized Iron Surfaces Studied by Atomic Force Microscopy and Polarization-Modulation Infrared Reflection Absorption Spectroscopy.” <i>Molecules</i> 28, no. 16 (2023). <a href=\"https://doi.org/10.3390/molecules28166060\">https://doi.org/10.3390/molecules28166060</a>."},"date_updated":"2023-08-16T10:53:08Z","intvolume":"        28","issue":"16","abstract":[{"lang":"eng","text":"<jats:p>Multiprotein adsorption from complex body fluids represents a highly important and complicated phenomenon in medicine. In this work, multiprotein adsorption from diluted human serum at gold and oxidized iron surfaces is investigated at different serum concentrations and pH values. Adsorption-induced changes in surface topography and the total amount of adsorbed proteins are quantified by atomic force microscopy (AFM) and polarization-modulation infrared reflection absorption spectroscopy (PM-IRRAS), respectively. For both surfaces, stronger protein adsorption is observed at pH 6 compared to pH 7 and pH 8. PM-IRRAS furthermore provides some qualitative insights into the pH-dependent alterations in the composition of the adsorbed multiprotein films. Changes in the amide II/amide I band area ratio and in particular side-chain IR absorption suggest that the increased adsorption at pH 6 is accompanied by a change in protein film composition. Presumably, this is mostly driven by the adsorption of human serum albumin, which at pH 6 adsorbs more readily and thereby replaces other proteins with lower surface affinities in the resulting multiprotein film.</jats:p>"}],"title":"Multiprotein Adsorption from Human Serum at Gold and Oxidized Iron Surfaces Studied by Atomic Force Microscopy and Polarization-Modulation Infrared Reflection Absorption Spectroscopy","author":[{"first_name":"Jingyuan","last_name":"Huang","full_name":"Huang, Jingyuan"},{"full_name":"Qiu, Yunshu","last_name":"Qiu","first_name":"Yunshu"},{"first_name":"Felix","last_name":"Lücke","full_name":"Lücke, Felix"},{"full_name":"Su, Jiangling","last_name":"Su","first_name":"Jiangling"},{"last_name":"Grundmeier","full_name":"Grundmeier, Guido","id":"194","first_name":"Guido"},{"id":"48864","first_name":"Adrian","last_name":"Keller","full_name":"Keller, Adrian","orcid":"0000-0001-7139-3110"}],"publication_identifier":{"issn":["1420-3049"]},"doi":"10.3390/molecules28166060","date_created":"2023-08-16T10:51:48Z","publication_status":"published","department":[{"_id":"302"}],"volume":28}