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Toward Activatable Collagen Mimics : Combining DEPSI "Switch" Defects and Template-Guided Self-Organization to Control Collagen Mimetic Peptides

Title data

Röber, Matthias ; Scheibel, Thomas ; Börner, Hans G.:
Toward Activatable Collagen Mimics : Combining DEPSI "Switch" Defects and Template-Guided Self-Organization to Control Collagen Mimetic Peptides.
In: Macromolecular Bioscience. (18 May 2021) .
ISSN 1616-5187
DOI: https://doi.org/10.1002/mabi.202100070

Abstract in another language

Collagen mimetic peptides (CMPs), which imitate various structural or functional features of natural collagen, constitute advanced models illuminating the folding aspects of the collagen triple helix (CTH) motif. In this study, the CMPs of repeating Gly–Pro–Pro (GPP) triplets are tethered to an organic scaffold based on a tris(2-aminoethyl) amine (TREN) derivative (TREN-(suc-OH)3). These three templated peptide strands are further expanded via native chemical ligation to increase the number of GPP triplets and lead to a TREN-(suc-GPPGPPG(Ψ)SPGPP-CPP[GPP]4)3 construct. The incorporation of an ester switch segment, G(Ψ)S, as a positional O-acyl isopeptide (DEPSI) defect into the peptide strands allows the pH-controlled acceleration of CTH formation. The strand assembly process is monitored by circular dichroism (CD) spectroscopy. The results of pH jump experiments and thermal denaturation studies provide new insights into the contributions of structural DEPSI defects to the template-guided self-assembly of the CTH motif. While the organic scaffold drives the CTH formation, the switch defects act as temporary opponents and slow down the folding. CD spectroscopy data confirm that the switch defects contribute to the formation of a more stable CTH motif by enhancing the structural dynamics at the early stage of the folding process.

Further data

Item Type: Article in a journal
Refereed: Yes
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: 13 Jul 2021 11:12
Last Modified: 13 Jul 2021 11:12
URI: https://eref.uni-bayreuth.de/id/eprint/66530