Stability Analysis of an Inline Peptide-based Conjugate for Metal Delivery: Nickel(II)-claMP Tag Epidermal Growth Factor as a Model System
dc.contributor.author | Mills, Brittney J. | |
dc.contributor.author | Laurence, Jennifer S. | |
dc.date.accessioned | 2017-04-26T17:32:06Z | |
dc.date.available | 2017-04-26T17:32:06Z | |
dc.date.issued | 2015-02 | |
dc.identifier.citation | Mills, B. J., & Laurence, J. S. (2015). Stability Analysis of an Inline Peptide-based Conjugate for Metal Delivery: Nickel(II)-claMP Tag Epidermal Growth Factor as a Model System. Journal of Pharmaceutical Sciences, 104(2), 416–423. http://doi.org/10.1002/jps.24132 | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/23813 | |
dc.description.abstract | Metals are a key component of many diagnostic imaging and biotechnology applications, and the majority of cancer patients receive a platinum-based drug as part of their treatment. Significant effort has been devoted to developing tight binding synthetic chelators to enable effective targeted delivery of metal-based conjugates, with most successes involving lanthanides rather than transition metals for diagnostic imaging. Chemical conjugation modifies the protein’s properties and generates a heterogeneous mixture of products. Chelator attachment is typically done by converting the amino group on lysines to an amide, which can impact the stability and solubility of the targeting protein and these properties vary among the set of individual conjugate species. Site-specific attachment is sought to reduce complexity and control stability. Here, the metal abstraction peptide (MAP) technology was applied to create the claMP Tag, an inline platform for generating site-specific conjugates involving transition metals. The claMP Tag was genetically encoded into epidermal growth factor (EGF) and loaded with nickel(II) as a model system to demonstrate that the tag within the homogeneous inline conjugate presents sufficient solution stability to enable biotechnology applications. The structure and disulfide network of the protein and chemical stability of the claMP Tag and EGF components were characterized. | en_US |
dc.publisher | Elsevier | en_US |
dc.rights | This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License 4.0 (CC BY-NC-ND 4.0), which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made. | en_US |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | en_US |
dc.subject | Protein structure | en_US |
dc.subject | Stability | en_US |
dc.subject | Conjugation | en_US |
dc.subject | Targeted drug delivery | en_US |
dc.subject | Metal abstraction peptide | en_US |
dc.subject | Map | en_US |
dc.subject | Absorption spectroscopy | en_US |
dc.subject | NMR | en_US |
dc.subject | Chromatography | en_US |
dc.subject | Analytical biochemistry | en_US |
dc.title | Stability Analysis of an Inline Peptide-based Conjugate for Metal Delivery: Nickel(II)-claMP Tag Epidermal Growth Factor as a Model System | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Mills, Brittany J. | |
kusw.kuauthor | Laurence, Jennifer S. | |
kusw.kudepartment | Pharmaceutical Chemistry | en_US |
kusw.kudepartment | Chemistry | en_US |
dc.identifier.doi | 10.1002/jps.24132 | en_US |
kusw.oaversion | Scholarly/refereed, author accepted manuscript | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC4312271 | en_US |
dc.rights.accessrights | openAccess |
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Except where otherwise noted, this item's license is described as: This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License 4.0 (CC BY-NC-ND 4.0), which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.