Screen-Based Analysis of Magnetic Nanoparticle Libraries Formed Using Peptidic Iron Oxide Ligands
The identification of effective polypeptide ligands for magnetic iron oxide nanoparticles (IONPs) could considerably accelerate the high-throughput analysis of IONP-based reagents for imaging and cell labeling. We developed a procedure for screening IONP ligands and applied it to compare candidate p...
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| Format: | Article |
| Language: | en_US |
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American Chemical Society (ACS)
2015
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| Online Access: | http://hdl.handle.net/1721.1/99460 https://orcid.org/0000-0002-2834-6359 https://orcid.org/0000-0003-2776-9509 https://orcid.org/0000-0002-5044-369X |
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| author | Barch, Mariya Okada, Satoshi Bartelle, Benjamin B. Jasanoff, Alan Pradip |
| author2 | Massachusetts Institute of Technology. Department of Biological Engineering |
| author_facet | Massachusetts Institute of Technology. Department of Biological Engineering Barch, Mariya Okada, Satoshi Bartelle, Benjamin B. Jasanoff, Alan Pradip |
| author_sort | Barch, Mariya |
| collection | MIT |
| description | The identification of effective polypeptide ligands for magnetic iron oxide nanoparticles (IONPs) could considerably accelerate the high-throughput analysis of IONP-based reagents for imaging and cell labeling. We developed a procedure for screening IONP ligands and applied it to compare candidate peptides that incorporated carboxylic acid side chains, catechols, and sequences derived from phage display selection. We found that only l-3,4-dihydroxyphenylalanine (DOPA)-containing peptides were sufficient to maintain particles in solution. We used a DOPA-containing sequence motif as the starting point for generation of a further library of over 30 peptides, each of which was complexed with IONPs and evaluated for colloidal stability and magnetic resonance imaging (MRI) contrast properties. Optimal properties were conferred by sequences within a narrow range of biophysical parameters, suggesting that these sequences could serve as generalizable anchors for formation of polypeptide–IONP complexes. Differences in the amino acid sequence affected T[subscript 1]- and T[subscript 2]-weighted MRI contrast without substantially altering particle size, indicating that the microstructure of peptide-based IONP coatings exerts a substantial influence and could be manipulated to tune properties of targeted or responsive contrast agents. A representative peptide–IONP complex displayed stability in biological buffer and induced persistent MRI contrast in mice, indicating suitability of these species for in vivo molecular imaging applications. |
| first_indexed | 2024-09-23T16:45:48Z |
| format | Article |
| id | mit-1721.1/99460 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T16:45:48Z |
| publishDate | 2015 |
| publisher | American Chemical Society (ACS) |
| record_format | dspace |
| spelling | mit-1721.1/994602022-09-29T21:19:28Z Screen-Based Analysis of Magnetic Nanoparticle Libraries Formed Using Peptidic Iron Oxide Ligands Barch, Mariya Okada, Satoshi Bartelle, Benjamin B. Jasanoff, Alan Pradip Massachusetts Institute of Technology. Department of Biological Engineering Massachusetts Institute of Technology. Department of Brain and Cognitive Sciences Massachusetts Institute of Technology. Department of Nuclear Science and Engineering Barch, Mariya Okada, Satoshi Bartelle, Benjamin B. Jasanoff, Alan Pradip The identification of effective polypeptide ligands for magnetic iron oxide nanoparticles (IONPs) could considerably accelerate the high-throughput analysis of IONP-based reagents for imaging and cell labeling. We developed a procedure for screening IONP ligands and applied it to compare candidate peptides that incorporated carboxylic acid side chains, catechols, and sequences derived from phage display selection. We found that only l-3,4-dihydroxyphenylalanine (DOPA)-containing peptides were sufficient to maintain particles in solution. We used a DOPA-containing sequence motif as the starting point for generation of a further library of over 30 peptides, each of which was complexed with IONPs and evaluated for colloidal stability and magnetic resonance imaging (MRI) contrast properties. Optimal properties were conferred by sequences within a narrow range of biophysical parameters, suggesting that these sequences could serve as generalizable anchors for formation of polypeptide–IONP complexes. Differences in the amino acid sequence affected T[subscript 1]- and T[subscript 2]-weighted MRI contrast without substantially altering particle size, indicating that the microstructure of peptide-based IONP coatings exerts a substantial influence and could be manipulated to tune properties of targeted or responsive contrast agents. A representative peptide–IONP complex displayed stability in biological buffer and induced persistent MRI contrast in mice, indicating suitability of these species for in vivo molecular imaging applications. National Institutes of Health (U.S.) (Grant R01-DA28299) National Institutes of Health (U.S.) (Grant R01-NS76462) National Institutes of Health (U.S.) (Grant R21-MH102470) Japan Society for the Promotion of Science (Postdoctoral Fellowship for Research Abroad) 2015-10-27T12:09:43Z 2015-10-27T12:09:43Z 2014-08 2013-10 Article http://purl.org/eprint/type/JournalArticle 0002-7863 1520-5126 http://hdl.handle.net/1721.1/99460 Barch, Mariya, Satoshi Okada, Benjamin B. Bartelle, and Alan Jasanoff. “Screen-Based Analysis of Magnetic Nanoparticle Libraries Formed Using Peptidic Iron Oxide Ligands.” Journal of the American Chemical Society 136, no. 36 (September 10, 2014): 12516–12519. © 2014 American Chemical Society https://orcid.org/0000-0002-2834-6359 https://orcid.org/0000-0003-2776-9509 https://orcid.org/0000-0002-5044-369X en_US http://dx.doi.org/10.1021/ja410884e Journal of the American Chemical Society Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf American Chemical Society (ACS) ACS |
| spellingShingle | Barch, Mariya Okada, Satoshi Bartelle, Benjamin B. Jasanoff, Alan Pradip Screen-Based Analysis of Magnetic Nanoparticle Libraries Formed Using Peptidic Iron Oxide Ligands |
| title | Screen-Based Analysis of Magnetic Nanoparticle Libraries Formed Using Peptidic Iron Oxide Ligands |
| title_full | Screen-Based Analysis of Magnetic Nanoparticle Libraries Formed Using Peptidic Iron Oxide Ligands |
| title_fullStr | Screen-Based Analysis of Magnetic Nanoparticle Libraries Formed Using Peptidic Iron Oxide Ligands |
| title_full_unstemmed | Screen-Based Analysis of Magnetic Nanoparticle Libraries Formed Using Peptidic Iron Oxide Ligands |
| title_short | Screen-Based Analysis of Magnetic Nanoparticle Libraries Formed Using Peptidic Iron Oxide Ligands |
| title_sort | screen based analysis of magnetic nanoparticle libraries formed using peptidic iron oxide ligands |
| url | http://hdl.handle.net/1721.1/99460 https://orcid.org/0000-0002-2834-6359 https://orcid.org/0000-0003-2776-9509 https://orcid.org/0000-0002-5044-369X |
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