The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Polyarginine enters cells more efficiently than other polycationic homopolymers
Abstract
Abstract: Homopolymers or peptides containing a high percentage of cationic amino acids have been shown to have a unique ability to cross the plasma membrane of cells, and consequently have been used to facilitate the uptake of a variety of biopolymers and small molecules. To investigate whether the polycationic character of these molecules, or some other structural feature, was the molecular basis for the effect, the ability of a variety of homopolymers to enter cells was assayed by confocal microscopy and flow cytometry. Polymers of l‐ or d‐arginine containing six or more amino acids entered cells far more effectively than polymers of equal length composed of lysine, ornithine and histidine. Peptides of fewer than six amino acids were ineffective. The length of the arginine side‐chain could be varied without significant loss of activity. These data combined with the inability of polymers of citrulline to enter cells demonstrated that the guanidine headgroup of arginine was the critical structural component responsible for the biological activity. Cellular uptake could be inhibited by pre‐incubation of the cells with sodium azide, but not by low temperature (3 °C), indicating that the process was energy dependent, but did not involve endocytosis.
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Cites
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Metadata
- Authors
- Mitchell, D. J., Steinman, L., Kim, D. T., Fathman, C. G., & Rothbard, J. B.
- Venue
- The Journal of Peptide Research
- Publisher
- Wiley
- Published
- 2000-11
- Volume
- 56
- Issue
- 5
- Pages
- 318-325
- ISSN
- 1397-002X (ISSN-L)
- OpenAlex
- W2111994795
- Cited by
- 1,084
- References
- 13
- FWCI
- 6.31
- Type
- journal article
- Language
- en
- Open access
- closed
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- Mitchell, D. J., Steinman, L., Kim, D. T., Fathman, C. G., & Rothbard, J. B. (2000). Polyarginine enters cells more efficiently than other polycationic homopolymers. The Journal of Peptide Research. https://doi.org/10.1034/j.1399-3011.2000.00723.x
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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