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. 2017 Dec 21;7:18041. doi: 10.1038/s41598-017-18029-y

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Scheme of site-specific palmitic acid-conjugation to urate oxidase (Uox) for acquired human serum albumin (HSA) binding capacity. A clickable non-natural amino acid, p-azido-L-phenylalanine (AzF) is introduced to a specific site of Uox. Palmitic acid analog containing dibenzocyclooctyne group (DBCO-Pal) is conjugated to AzF site of Uox via strain-promoted azide-alkyne cycloaddition (SPAAC). The palmitic acid-conjugated Uox (Uox-Pal) binds HSA, while wild-type Uox (Uox-WT) does not bind HSA. In the structure of Uox, AzF incorporation site and active site, which are marked in blue and red respectively, are distant from each other.