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New Compstatin Peptides Containing N-Terminal Extensions and Non-Natural Amino Acids Exhibit Potent Complement Inhibition and Improved Solubility Characteristics
[Image: see text] Compstatin peptides are complement inhibitors that bind and inhibit cleavage of complement C3. Peptide binding is enhanced by hydrophobic interactions; however, poor solubility promotes aggregation in aqueous environments. We have designed new compstatin peptides derived from the W...
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| Pubblicato in: | J Med Chem |
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| Autori principali: | , , , , , , , , , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
American Chemical
Society
2014
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| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4306506/ https://ncbi.nlm.nih.gov/pubmed/25494040 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/jm501345y |
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