English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  In silico and NMR identification of inhibitors of the IGF-I and IGF-binding protein-5 interaction

Kamionka, M., Rehm, T., Beisel, H. G., Lang, K., Engh, R. A., & Holak, T. A. (2002). In silico and NMR identification of inhibitors of the IGF-I and IGF-binding protein-5 interaction. Journal of Medicinal Chemistry, 45(26), 5655-5660.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : J. Med. Chem.

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Kamionka, M., Author
Rehm, T.1, Author           
Beisel, H. G.2, Author           
Lang, K., Author
Engh, R. A.3, Author           
Holak, T. A.2, Author           
Affiliations:
1External Organizations, ou_persistent22              
2Holak, Tad / NMR Spectroscopy, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565154              
3Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              

Content

show
hide
Free keywords: -
 Abstract: Recently we have determined the crystal structure of the insulin-like growth factor-I (IGF-I) in complex with the N- terminal domain of the IGF-binding protein-5 (IGFBP-5). Here we report results of computer screening for potential inhibitors of this interaction using the crystal coordinates. From the compounds suggested by in silico screens, successful binders were identified by NMR spectroscopic methods. NMR was also used to map their binding sites and calculate their binding affinities. Small molecular weight compounds (FMOC derivatives) bind to the IGF-I binding site on the IGFBP-5 with micromolar affinities and thus serve as potential starting compounds for the design of more potent inhibitors and therapeutic agents for diseases that are associated with abnormal IGF-I regulation.

Details

show
hide
Language(s): eng - English
 Dates: 2002-12-19
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41729
ISI: 000179814800008
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Medicinal Chemistry
  Alternative Title : J. Med. Chem.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 45 (26) Sequence Number: - Start / End Page: 5655 - 5660 Identifier: ISSN: 0022-2623