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Modulating the collagen triple helix formation by switching : Positioning effects of depsi-defects on the assembly of [Gly-Pro-Pro]7 collagen mimetic peptides

Title data

Röber, Matthias ; Laroque, Sophie ; Scheibel, Thomas ; Börner, Hans G.:
Modulating the collagen triple helix formation by switching : Positioning effects of depsi-defects on the assembly of [Gly-Pro-Pro]7 collagen mimetic peptides.
In: European Polymer Journal. Vol. 112 (March 2019) . - pp. 301-305.
ISSN 0014-3057
DOI: https://doi.org/10.1016/j.eurpolymj.2018.12.045

Abstract in another language

Collagen mimetic peptides (CMPs) based on repeating triads of [Gly-Pro-Pro] are guided by an N-terminally located SWCGTTPGSWCGT domain (cysteine rich wc2-knot foldon) to form collagen triple helix (CTH) motifs. The implementation of depsi “switch” defects into the peptide sequence SWCGTTPGSWCGT-[GPP]7 (wc2-[GPP]7) is disturbing the CTH formation at pH ≤ 5.5. Whereas upon pH increase to pH = 7.4 a rapid O → N-acyl transfer rearrangement takes place. This reinstalls the native amide backbone structure and contributes to the acceleration of the CTH formation. A set of wc2-[GPP]7 constructs is synthesized and “switch” defect segments are positioned either C-terminal, or N-terminal and at both termini. Circular dichroism (CD) spectroscopy in combination with CTH melting studies allows to investigate the effect of defect positioning on wc2-foldon organization, [GPP]7 triple helix motif formation and the respective thermal stability of the resulting CTH structures. C-terminal defects improve the anticipated zipper-like process of the wc2-guided CTH formation, whereas N-terminal defects are more disturbing the structure formation by interfering with the wc2-domain organization.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: Collagen; Triple helix; Self-assembly; Collagen mimetic peptides; pH switch
DEPSI peptides
Institutions of the University: Faculties
Faculties > Faculty of Engineering Science
Faculties > Faculty of Engineering Science > Chair Biomaterials
Faculties > Faculty of Engineering Science > Chair Biomaterials > Chair Biomaterials - Univ.-Prof. Dr. Thomas Scheibel
Profile Fields
Profile Fields > Advanced Fields
Profile Fields > Advanced Fields > Polymer and Colloid Science
Profile Fields > Advanced Fields > Advanced Materials
Profile Fields > Advanced Fields > Molecular Biosciences
Profile Fields > Emerging Fields
Profile Fields > Emerging Fields > Food and Health Sciences
Research Institutions
Research Institutions > Research Centres
Research Institutions > Research Centres > Bayreuth Center for Material Science and Engineering - BayMAT
Result of work at the UBT: Yes
DDC Subjects: 600 Technology, medicine, applied sciences
600 Technology, medicine, applied sciences > 620 Engineering
Date Deposited: 20 Jan 2020 11:34
Last Modified: 20 Jan 2020 11:34
URI: https://eref.uni-bayreuth.de/id/eprint/54141