at Google ScholarTitle 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
(2019)
.
- pp. 301-305.
ISSN 1873-1945
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.