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2021-05-18Zeitschriftenartikel DOI: 10.1002/mabi.202100070
Toward Activatable Collagen Mimics: Combining DEPSI “Switch” Defects and Template‐Guided Self‐Organization to Control Collagen Mimetic Peptides
dc.contributor.authorRöber, Matthias
dc.contributor.authorScheibel, Thomas
dc.contributor.authorBörner, Hans G.
dc.date.accessioned2021-10-19T08:33:56Z
dc.date.available2021-10-19T08:33:56Z
dc.date.issued2021-05-18none
dc.date.updated2021-09-08T01:55:44Z
dc.identifier.urihttp://edoc.hu-berlin.de/18452/24232
dc.description.abstractCollagen 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.eng
dc.language.isoengnone
dc.publisherHumboldt-Universität zu Berlin
dc.rights(CC BY-NC 4.0) Attribution-NonCommercial 4.0 Internationalger
dc.rights.urihttps://creativecommons.org/licenses/by-nc/4.0/
dc.subjectcollagen mimetic peptideseng
dc.subjectcollagen triple helixeng
dc.subjectself‐organizationeng
dc.subject.ddc570 Biologienone
dc.titleToward Activatable Collagen Mimics: Combining DEPSI “Switch” Defects and Template‐Guided Self‐Organization to Control Collagen Mimetic Peptidesnone
dc.typearticle
dc.identifier.urnurn:nbn:de:kobv:11-110-18452/24232-2
dc.identifier.doi10.1002/mabi.202100070none
dc.identifier.doihttp://dx.doi.org/10.18452/23578
dc.type.versionpublishedVersionnone
local.edoc.container-titleMacromolecular Biosciencenone
local.edoc.pages7none
local.edoc.type-nameZeitschriftenartikel
local.edoc.institutionMathematisch-Naturwissenschaftliche Fakultätnone
local.edoc.container-typeperiodical
local.edoc.container-type-nameZeitschrift
local.edoc.container-publisher-nameWiley-VCHnone
local.edoc.container-publisher-placeWeinheimnone
local.edoc.container-volume21none
local.edoc.container-issue7none
dc.description.versionPeer Reviewednone
local.edoc.container-articlenumber2100070none
dc.identifier.eissn1616-5195
local.edoc.affiliationRöber, Matthias; 1 Laboratory for Organic Synthesis of Functional Systems Department of Chemistry Humboldt Universität zu Berlin Brook‐Taylor‐Str. 2 Berlin 12489 Germanynone
local.edoc.affiliationScheibel, Thomas; 2 Lehrstuhl Biomaterialien, Fakultät für Ingenieurwissenschaften Universität Bayreuth Universitätsstraße 30 Bayreuth D‐95440 Germanynone

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