dc.contributor.author | Gorham, R. D. | en |
dc.contributor.author | Forest, D. L. | en |
dc.contributor.author | Khoury, G. A. | en |
dc.contributor.author | Smadbeck, J. | en |
dc.contributor.author | Beecher, C. N. | en |
dc.contributor.author | Healy, E. D. | en |
dc.contributor.author | Tamamis, Phanourios | en |
dc.contributor.author | Archontis, Georgios Z. | en |
dc.contributor.author | Larive, C. K. | en |
dc.contributor.author | Floudas, C. A. | en |
dc.contributor.author | Radeke, M. J. | en |
dc.contributor.author | Johnson, L. V. | en |
dc.contributor.author | Morikis, D. | en |
dc.creator | Gorham, R. D. | en |
dc.creator | Forest, D. L. | en |
dc.creator | Khoury, G. A. | en |
dc.creator | Smadbeck, J. | en |
dc.creator | Beecher, C. N. | en |
dc.creator | Healy, E. D. | en |
dc.creator | Tamamis, Phanourios | en |
dc.creator | Archontis, Georgios Z. | en |
dc.creator | Larive, C. K. | en |
dc.creator | Floudas, C. A. | en |
dc.creator | Radeke, M. J. | en |
dc.creator | Johnson, L. V. | en |
dc.creator | Morikis, D. | en |
dc.date.accessioned | 2019-12-02T15:30:24Z | |
dc.date.available | 2019-12-02T15:30:24Z | |
dc.date.issued | 2015 | |
dc.identifier.uri | http://gnosis.library.ucy.ac.cy/handle/7/58697 | |
dc.description.abstract | Compstatin peptides are complement inhibitors that bind and inhibit cleavage of complement C3. Peptide binding is enhanced by hydrophobic interactions | en |
dc.description.abstract | however, poor solubility promotes aggregation in aqueous environments. We have designed new compstatin peptides derived from the W4A9 sequence (Ac-ICVWQDWGAHRCT-NH2, cyclized between C2 and C12), based on structural, computational, and experimental studies. Furthermore, we developed and utilized a computational framework for the design of peptides containing non-natural amino acids. These new compstatin peptides contain polar N-terminal extensions and non-natural amino acid substitutions at positions 4 and 9. Peptides with α-modified non-natural alanine analogs at position 9, as well as peptides containing only N-terminal polar extensions, exhibited similar activity compared to W4A9, as quantified via ELISA, hemolytic, and cell-based assays, and showed improved solubility, as measured by UV absorbance and reverse-phase HPLC experiments. Because of their potency and solubility, these peptides are promising candidates for therapeutic development in numerous complement-mediated diseases. © 2014 American Chemical Society. | en |
dc.source | Journal of medicinal chemistry | en |
dc.source.uri | https://www.scopus.com/inward/record.uri?eid=2-s2.0-84921456708&doi=10.1021%2fjm501345y&partnerID=40&md5=7ba970546402025da261d8a7a77fb84c | |
dc.subject | human | en |
dc.subject | Humans | en |
dc.subject | controlled study | en |
dc.subject | amino acid sequence | en |
dc.subject | unclassified drug | en |
dc.subject | nonhuman | en |
dc.subject | Article | en |
dc.subject | high performance liquid chromatography | en |
dc.subject | molecular genetics | en |
dc.subject | human cell | en |
dc.subject | Animals | en |
dc.subject | complement inhibitor | en |
dc.subject | animal | en |
dc.subject | animal cell | en |
dc.subject | Molecular Sequence Data | en |
dc.subject | in vitro study | en |
dc.subject | chemistry | en |
dc.subject | drug effects | en |
dc.subject | Rabbits | en |
dc.subject | drug solubility | en |
dc.subject | enzyme linked immunosorbent assay | en |
dc.subject | hemolysis | en |
dc.subject | synthesis | en |
dc.subject | amino acid | en |
dc.subject | solubility | en |
dc.subject | rabbit | en |
dc.subject | molecular dynamics | en |
dc.subject | amino terminal sequence | en |
dc.subject | cell culture | en |
dc.subject | amino acid substitution | en |
dc.subject | pigment epithelium | en |
dc.subject | structure activity relation | en |
dc.subject | Cells, Cultured | en |
dc.subject | hydrophobicity | en |
dc.subject | complement component C3b | en |
dc.subject | complement component C5b | en |
dc.subject | Complement Inactivating Agents | en |
dc.subject | complement inhibition | en |
dc.subject | compstatin | en |
dc.subject | compstatin peptide | en |
dc.subject | cyclopeptide | en |
dc.subject | drug binding site | en |
dc.subject | lipophilicity | en |
dc.subject | peptide synthesis | en |
dc.subject | Peptides, Cyclic | en |
dc.subject | Retinal Pigment Epithelium | en |
dc.title | New compstatin peptides containing n-terminal extensions and non-natural amino acids exhibit potent complement inhibition and improved solubility characteristics | en |
dc.type | info:eu-repo/semantics/article | |
dc.identifier.doi | 10.1021/jm501345y | |
dc.description.volume | 58 | |
dc.description.issue | 2 | |
dc.description.startingpage | 814 | |
dc.description.endingpage | 826 | |
dc.author.faculty | Σχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences | |
dc.author.department | Τμήμα Φυσικής / Department of Physics | |
dc.type.uhtype | Article | en |
dc.description.notes | <p>Cited By :5</p> | en |
dc.source.abbreviation | J.Med.Chem. | en |
dc.contributor.orcid | Tamamis, Phanourios [0000-0002-3342-2651] | |
dc.contributor.orcid | Archontis, Georgios Z. [0000-0002-7750-8641] | |
dc.gnosis.orcid | 0000-0002-3342-2651 | |
dc.gnosis.orcid | 0000-0002-7750-8641 | |