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DC Field | Value | Language |
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dc.citation.endPage | 225 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 219 | - |
dc.citation.title | JOURNAL OF CONTROLLED RELEASE | - |
dc.citation.volume | 170 | - |
dc.contributor.author | Lim, Sung In | - |
dc.contributor.author | Mizuta, Yukina | - |
dc.contributor.author | Takasu, Akinori | - |
dc.contributor.author | Hahn, Young S. | - |
dc.contributor.author | Kim, Yong Hwan | - |
dc.contributor.author | Kwon, Inchan | - |
dc.date.accessioned | 2023-12-22T03:37:33Z | - |
dc.date.available | 2023-12-22T03:37:33Z | - |
dc.date.created | 2016-09-06 | - |
dc.date.issued | 2013-09 | - |
dc.description.abstract | Therapeutic proteins are indispensable in treating numerous human diseases. However, therapeutic proteins often suffer short serum half-life. In order to extend the serum half-life, a natural albumin ligand (a fatty acid) has been conjugated to small therapeutic peptides resulting in a prolonged serum half-life via binding to patients' serum albumin in vivo. However, fatty acid-conjugation has limited applicability due to lack of site-specificity resulting in the heterogeneity of conjugated proteins and a significant loss in pharmaceutical activity. In order to address these issues, we exploited the site-specific fatty acid-conjugation to a permissive site of a protein, using copper-catalyzed alkyne-azide cycloaddition, by linking a fatty acid derivative to p-ethynylphenylalanine incorporated into a protein using an engineered pair of yeast tRNA/aminoacyl tRNA synthetase. As a proof-of-concept, we show that single palmitic acid conjugated to superfolder green fluorescent protein (sfGFP) in a site-specific manner enhanced a protein's albumin-binding in vitro about 20 times and the serum half-life in vivo 5 times when compared to those of the unmodified sfGFP. Furthermore, the fatty acid conjugation did not cause a significant reduction in the fluorescence of sfGFP. Therefore, these results clearly indicate that the site-specific fatty acid-conjugation is a very promising strategy to prolong protein serum half-life in vivo without compromising its folded structure and activity. | - |
dc.identifier.bibliographicCitation | JOURNAL OF CONTROLLED RELEASE, v.170, no.2, pp.219 - 225 | - |
dc.identifier.doi | 10.1016/j.jconrel.2013.05.023 | - |
dc.identifier.issn | 0168-3659 | - |
dc.identifier.scopusid | 2-s2.0-84879477738 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/20352 | - |
dc.identifier.url | http://www.sciencedirect.com/science/article/pii/S0168365913003131 | - |
dc.identifier.wosid | 000321747200008 | - |
dc.language | 영어 | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.title | Site-specific fatty acid-conjugation to prolong protein half-life in vivo | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | Noncanonical amino acid | - |
dc.subject.keywordAuthor | Fatty acid | - |
dc.subject.keywordAuthor | Copper-catalyzed alkyne-azide cycloaddition | - |
dc.subject.keywordAuthor | Albumin | - |
dc.subject.keywordAuthor | Half-life | - |
dc.subject.keywordPlus | ALBUMIN-BINDING DOMAIN | - |
dc.subject.keywordPlus | SINGLE-CHAIN DIABODY | - |
dc.subject.keywordPlus | GENETIC-CODE | - |
dc.subject.keywordPlus | FUSION PROTEIN | - |
dc.subject.keywordPlus | AMINO-ACID | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | SERUM-ALBUMIN | - |
dc.subject.keywordPlus | RECOMBINANT PROTEINS | - |
dc.subject.keywordPlus | BACTERIAL-CELLS | - |
dc.subject.keywordPlus | LONG | - |
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