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Main Title: Promotion of the collagen triple helix in a hydrophobic environment
Author(s): Kubyshkin, Vladimir
Budisa, Nediljko
Type: Article
Language Code: en
Abstract: In contrast to many other water-soluble peptide arrangements, the formation of a triple helix in collagen proceeds inside out: polar glycyl residues form the interior, whereas nonpolar prolyl side chains constitute the exterior. In our work, we decided to exploit this aspect of the peptide architecture in order to create hyperstable collagen mimicking peptides (CMPs). The key element of this study is the environment. Given that the peptide assembles in a nonpolar medium, the collapse of the polar peptide backbone into the triple helix should become more favorable. Following this idea, we prepared CMPs based on hydrophobic proline analogues. The synthesis was performed by a combination of liquid- and solid-phase approaches: first, hexapeptides were prepared in solution, and then these were launched into conventional Fmoc-based peptide synthesis on a solid support. The resulting peptides showed an excellent signal of the triple helix in the model nonpolar solvent (octanol) according to circular dichroism observations. In a study of a series of oligomers, we found that the minimal length of the peptides required for triple helical assembly is substantially lower compared to water-soluble CMPs. Our results suggest further explorations of the CMPs in hydrophobic media; in particular, we highlight the suggestion that collagen could be converted into a membrane protein.
Issue Date: 6-Feb-2019
Date Available: 30-Apr-2019
DDC Class: 540 Chemie und zugeordnete Wissenschaften
Sponsor/Funder: DFG, 207100805, FOR 1805: Einfluss der Ribosomendynamik auf Regulation der Geschwindigkeit und Genauigkeit der Translation
TU Berlin, Open-Access-Mittel - 2019
Journal Title: Organic & Biomolecular Chemistry
Publisher: Royal Society of Chemistry
Publisher Place: Cambridge
Volume: 17
Issue: 9
Publisher DOI: 10.1039/C9OB00070D
Page Start: 2502
Page End: 2507
EISSN: 1477-0539
ISSN: 1477-0520
Appears in Collections:FG Biokatalyse » Publications

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