Cyclopeptides containing the DEKS motif as conformationally restricted collagen telopeptide analogues: synthesis and conformational analysis-Reference-Cited by-同舟云学术

Cyclopeptides containing the DEKS motif as conformationally restricted collagen telopeptide analogues: synthesis and conformational analysis

Published:2015 Issue:6 Volume:13 Page:1878-1896
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Wodtke Robert¹²³⁴⁵,Ruiz-Gómez Gloria⁶⁷⁸⁹⁴,Kuchar Manuela¹²³⁴⁵,Pisabarro M. Teresa⁶⁷⁸⁹⁴,Novotná Pavlina¹⁰¹¹¹²¹³,Urbanová Marie¹⁰¹¹¹²¹³,Steinbach Jörg¹²³⁴⁵,Pietzsch Jens¹²³⁴⁵,Löser Reik¹²³⁴⁵

Affiliation:

1. Institute of Radiopharmaceutical Cancer Research

2. Helmholtz-Zentrum Dresden-Rossendorf

3. 01328 Dresden

4. Germany

5. Department of Chemistry and Food Chemistry

6. Structural Bioinformatics

7. BIOTEC

8. Technische Universität Dresden

9. 01307 Dresden

10. Department of Physics and Measurements

11. Institute of Chemical Technology

12. 166 28 Prague

13. Czech Republic

Abstract

The conformational stabilisation of the DEKS motif at the α1(I) collagenN-telopeptide within a cyclic hexapeptide together with its conformational analysis is described. This sequence is critical for lysyl oxidase-mediated collagen crosslinking, a process which is deregulated during tumour progression.

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2015/OB/C4OB02348J

Reference81 articles.

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4. Type I collagen N-Telopeptides adopt an ordered structure when docked to their helix receptor during fibrillogenesis*

5. Lysyl oxidase is essential for hypoxia-induced metastasis

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