Skip Navigation


PEDS Advance Access originally published online on July 2, 2004
Protein Engineering Design and Selection 2004 17(5):433-441; doi:10.1093/protein/gzh055
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
17/5/433    most recent
gzh055v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (11)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Hölig, P.
Right arrow Articles by Kontermann, R. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hölig, P.
Right arrow Articles by Kontermann, R. E.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Protein Engineering, Design & Selection vol. 17 no. 5 © Oxford University Press 2004; all rights reserved

Novel RGD lipopeptides for the targeting of liposomes to integrin-expressing endothelial and melanoma cells

Peter Hölig1, Miriam Bach1, Tina Völkel1, Thomas Nahde1, Sven Hoffmann1, Rolf Müller2 and Roland E. Kontermann1,3

1Vectron Therapeutics AG, Rudolf-Breitscheid-Strasse 24, 35037 Marburg, Germany and 2Institut für Molekularbiologie und Tumorforschung, Philipps-Universität, Emil-Mannkopff-Strasse 2, 35033 Marburg, Germany

3 To whom correspondence should be addressed. E-mail: kontermann{at}aol.com

RGD peptides targeting {alpha}v-integrins are promising ligands for the generation of vascular targeting agents. We isolated from phage display RGD motif libraries novel high-affinity cyclic RGD peptides by selection on either endothelial or melanoma cells. Although the starting sequences contained only two cysteine residues flanking the RGD motif, several of the isolated peptides possessed four cysteine residues. A high-affinity peptide (RGD10) constrained by only one disulfide bond was used to generate novel lipopeptides composed of a lipid anchor, a short flexible spacer and the peptide ligand conjugated to the spacer end. Incorporation of RGD10 lipopeptides into liposomes resulted in specific and efficient binding of the liposomes to integrin-expressing cells. In vivo experiments applying doxorubicin-loaded RGD10 liposomes in a C26 colon carcinoma mouse model demonstrated improved efficacy compared with free doxorubicin and untargeted liposomes.

Received February 24, 2004; revised May 17, 2004; accepted May 21, 2004.

Edited by Bernd Gutte


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 FASEB J.Home page
P. M. Winter, A. H. Schmieder, S. D. Caruthers, J. L. Keene, H. Zhang, S. A. Wickline, and G. M. Lanza
Minute dosages of {alpha}{nu}{beta}3-targeted fumagillin nanoparticles impair Vx-2 tumor angiogenesis and development in rabbits
FASEB J, August 1, 2008; 22(8): 2758 - 2767.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
J. Meng, N. Ma, Z. Yan, W. Han, and Y. Zhang
NGR Enhanced the Anti-Angiogenic Activity of tum-5
J. Biochem., August 1, 2006; 140(2): 299 - 304.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.