Skip to main content

Novel compstatin family peptides inhibit complement activation by drusen-like deposits in human retinal pigmented epithelial cell cultures

Author(s): Gorham, Ronald D; Forest, David L; Tamamis, Phanourios; López de Victoria, Aliana; Kraszni, Márta; et al

Download
To refer to this page use: http://arks.princeton.edu/ark:/88435/pr1bg3q
Full metadata record
DC FieldValueLanguage
dc.contributor.authorGorham, Ronald D-
dc.contributor.authorForest, David L-
dc.contributor.authorTamamis, Phanourios-
dc.contributor.authorLópez de Victoria, Aliana-
dc.contributor.authorKraszni, Márta-
dc.contributor.authorKieslich, Chris A-
dc.contributor.authorBanna, Christopher D-
dc.contributor.authorBellows-Peterson, Meghan L-
dc.contributor.authorLarive, Cynthia K-
dc.contributor.authorFloudas, Christodoulos A-
dc.contributor.authorArchontis, Georgios-
dc.contributor.authorJohnson, Lincoln V-
dc.contributor.authorMorikis, Dimitrios-
dc.date.accessioned2021-10-08T19:58:54Z-
dc.date.available2021-10-08T19:58:54Z-
dc.date.issued2013en_US
dc.identifier.citationGorham Jr, Ronald D., David L. Forest, Phanourios Tamamis, Aliana López de Victoria, Márta Kraszni, Chris A. Kieslich, Christopher D. Banna, Meghan L. Bellows-Peterson, Cynthia K. Larive, Christodoulos A. Floudas, Georgios Archontis, Lincoln V. Johnson, and Dimitrios Morikis. "Novel compstatin family peptides inhibit complement activation by drusen-like deposits in human retinal pigmented epithelial cell cultures." Experimental Eye Research 116 (2013): 96-108. doi: 10.1016/j.exer.2013.07.023en_US
dc.identifier.issn0014-4835-
dc.identifier.urihttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3840162/-
dc.identifier.urihttp://arks.princeton.edu/ark:/88435/pr1bg3q-
dc.description.abstractWe have used a novel human retinal pigmented epithelial (RPE) cell-based model that mimics drusen biogenesis and the pathobiology of age-related macular degeneration to evaluate the efficacy of newly designed peptide inhibitors of the complement system. The peptides belong to the compstatin family and, compared to existing compstatin analogs, have been optimized to promote binding to their target, complement protein C3, and to enhance solubility by improving their polarity/hydrophobicity ratios. Based on analysis of molecular dynamics simulation data of peptide–C3 complexes, novel binding features were designed by introducing intermolecular salt bridge-forming arginines at the N-terminus and at position −1 of N-terminal dipeptide extensions. Our study demonstrates that the RPE cell assay has discriminatory capability for measuring the efficacy and potency of inhibitory peptides in a macular disease environment.en_US
dc.format.extent96 - 108en_US
dc.language.isoen_USen_US
dc.relation.ispartofExperimental Eye Researchen_US
dc.rightsAuthor's manuscripten_US
dc.titleNovel compstatin family peptides inhibit complement activation by drusen-like deposits in human retinal pigmented epithelial cell culturesen_US
dc.typeJournal Articleen_US
dc.identifier.doidoi:10.1016/j.exer.2013.07.023-
pu.type.symplectichttp://www.symplectic.co.uk/publications/atom-terms/1.0/journal-articleen_US

Files in This Item:
File Description SizeFormat 
CompstatinInhibitComplementDrusenDeposit.pdf3.53 MBAdobe PDFView/Download


Items in OAR@Princeton are protected by copyright, with all rights reserved, unless otherwise indicated.