The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Protein Modification, Bioconjugation, and Disulfide Bridging Using Bromomaleimides
Open accessAbstract
The maleimide motif is widely used for the selective chemical modification of cysteine residues in proteins. Despite widespread utilization, there are some potential limitations, including the irreversible nature of the reaction and, hence, the modification and the number of attachment positions. We conceived of a new class of maleimide which would address some of these limitations and provide new opportunities for protein modification. We report herein the use of mono- and dibromomaleimides for reversible cysteine modification and illustrate this on the SH2 domain of the Grb2 adaptor protein (L111C). After initial modification of a protein with a bromo- or dibromomaleimide, it is possible to add an equivalent of a second thiol to give further bioconjugation, demonstrating that bromomaleimides offer opportunities for up to three points of attachment. The resultant protein-maleimide products can be cleaved to regenerate the unmodified protein by addition of a phosphine or a large excess of a thiol. Furthermore, dibromomaleimide can insert into a disulfide bond, forming a maleimide bridge, and this is illustrated on the peptide hormone somatostatin. Fluorescein-labeled dibromomaleimide is synthesized and inserted into the disulfide to construct a fluorescent somatostatin analogue. These results highlight the significant potential for this new class of reagents in protein modification.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Schafer, F. Q., & Buettner, G. R. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00480-4 · Cited by 4,587
Saito, G., Swanson, J. A., & Lee, K.-D. (2003) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00179-5 · Cited by 1,407
(1997) · General Pharmacology: The Vascular System · doi:10.1016/s0306-3623(97)89864-3 · Cited by 750
Chemical Modification of Proteins at Cysteine: Opportunities in Chemistry and Biology
Chalker, J. M., Bernardes, G. J. L., Lin, Y. A., & Davis, B. G. (2009) · Chemistry – An Asian Journal · doi:10.1002/asia.200800427 · Cited by 649
The Stability of N-Ethylmaleimide and its Reaction with Sulfhydryl Groups
Gregory, J. D. (1955) · Journal of the American Chemical Society · doi:10.1021/ja01619a073 · Cited by 345
Somatostatin Analogs in Acromegaly
Freda, P. U. (2002) · Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.87.7.3013 · Cited by 298
Occurrence, conformational features and amino acid propensities for the π-helix
Fodje, M. N., & Al-Karadaghi, S. (2002) · Protein Engineering, Design and Selection · doi:10.1093/protein/15.5.353 · Cited by 264
Site-specific PEGylation of native disulfide bonds in therapeutic proteins
Shaunak, S., Godwin, A., Choi, J.-W., Balan, S., Pedone, E., Vijayarangam, D., Heidelberger, S., Teo, I., Zloh, M., & Brocchini, S. (2006) · Nature Chemical Biology · doi:10.1038/nchembio786 · Cited by 261
Disulfide bridge based PEGylation of proteins
Brocchini, S., Godwin, A., Balan, S., Choi, J.-W., Zloh, M., & Shaunak, S. (2008) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2007.06.014 · Cited by 186
Site-Specific PEGylation of Protein Disulfide Bonds Using a Three-Carbon Bridge
Balan, S., Choi, J.-W., Godwin, A., Teo, I., Laborde, C. M., Heidelberger, S., Zloh, M., Shaunak, S., & Brocchini, S. (2007) · Bioconjugate Chemistry · doi:10.1021/bc0601471 · Cited by 172
Vanderhooft, J. L., Mann, B. K., & Prestwich, G. D. (2007) · Biomacromolecules · doi:10.1021/bm0703564 · Cited by 124
Bednar, R. A. (1990) · Biochemistry · doi:10.1021/bi00467a014 · Cited by 124
Bromomaleimides: new reagents for the selective and reversible modification of cysteine
Tedaldi, L. M., Smith, M. E. B., Nathani, R. I., & Baker, J. R. (2009) · Chemical Communications · doi:10.1039/b915136b · Cited by 108
Self-citationSynthesis of substituted bis(heteroaryl)maleimides
Dubernet, M., Caubert, V., Guillard, J., & Viaud‐Massuard, M. (2005) · Tetrahedron · doi:10.1016/j.tet.2005.03.016 · Cited by 66
Somatostatin analog octreotide LAR®in gastro–entero–pancreatic tumors
Öberg, K. (2009) · Expert Review of Anticancer Therapy · doi:10.1586/era.09.26 · Cited by 33
Cited by
Antibody drug conjugate: the “biological missile” for targeted cancer therapy
Fu, Z., Li, S., Han, S., Shi, C., & Zhang, Y. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00947-7 · Cited by 1,643
Polymer–drug conjugate therapeutics: advances, insights and prospects
Ekladious, I., Colson, Y. L., & Grinstaff, M. W. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-018-0005-0 · Cited by 855
Therapeutic Protein–Polymer Conjugates: Advancing Beyond PEGylation
Pelegri-O’Day, E. M., Lin, E.-W., & Maynard, H. D. (2014) · Journal of the American Chemical Society · doi:10.1021/ja504390x · Cited by 622
Metal–Organic Frameworks for Cell and Virus Biology: A Perspective
Riccò, R., Liang, W., Li, S., Gassensmith, J. J., Caruso, F., Doonan, C., & Falcaro, P. (2018) · ACS Nano · doi:10.1021/acsnano.7b08056 · Cited by 293
Allenamides as Orthogonal Handles for Selective Modification of Cysteine in Peptides and Proteins
Abbas, A., Xing, B., & Loh, T. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201403121 · Cited by 117
Metadata
- Authors
- Smith, M. E. B., Schumacher, F. F., Ryan, C. P., Tedaldi, L. M., Papaioannou, D., Waksman, G., Caddick, S., & Baker, J. R.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-01-21
- Volume
- 132
- Issue
- 6
- Pages
- 1960-1965
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2061020069
- Cited by
- 377
- References
- 15
- FWCI
- 8.84
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
