Search results for "Triple Helix"

showing 3 items of 13 documents

Procollagen C-proteinase Enhancer Stimulates Procollagen Processing by Binding to the C-propeptide Region Only*

2011

Background: Procollagen C-proteinase enhancer-1 (PCPE-1) is an extracellular glycoprotein that increases activity of certain zinc metalloproteinases involved in tissue development and repair. Results: PCPE-1 binds uniquely to the C-propeptide region of the procollagen molecule. Conclusion: PCPE-1 enhances proteolysis by binding solely to the procollagen C-propeptides. Significance: These data may lead to future applications in the development of antifibrotic therapies.

animal structuresGlycosylationBiologyBiochemistryBone morphogenetic protein 1Protein Structure SecondaryBone Morphogenetic Protein 103 medical and health scienceschemistry.chemical_compoundMetalloprotease0302 clinical medicineHumansBinding siteEnhancerMolecular Biology030304 developmental biologyCell Line TransformedGlycoproteinschemistry.chemical_classification0303 health sciencesMetalloproteinaseExtracellular Matrix ProteinsBinding Sitesintegumentary systemCell BiologyEnzymatic ProcessingFibrosisExtracellular MatrixProcollagen peptidaseCollagen Type IIIchemistryBiochemistry030220 oncology & carcinogenesisembryonic structuresEnzymologyCollagenGlycoproteinProtein Processing Post-TranslationalTriple helixThe Journal of Biological Chemistry
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Morphological transformations in a dually thermoresponsive coil-rod-coil bioconjugate.

2013

We report the conformational and assembly behavior of a thermoresponsive triblock biohybrid conjugate under aqueous conditions. The triblock comprises of poly(diethylene glycol methyl ether methacrylate) (PDEGMEMA) conjugated to the ends of a triple-helix forming collagen-like peptide. The circular dichroism (CD) experiment confirms the ability of the collagen-like peptide middle block to assemble as a triple helix in the hybrid conjugate. Above the LCST (∼35 °C), the collapse of the thermoresponsive PDEGMEMA polymer at the ends of the peptide domain resulted in a concomitant increase in the conformational stability of the peptide domain towards thermal denaturation. Upon cooling back, the …

chemistry.chemical_classificationCircular dichroismChemistryGeneral ChemistryPolymerCondensed Matter PhysicsMethacrylateLower critical solution temperatureArticleCrystallographyTransmission electron microscopyPolymer chemistryStatic light scatteringConjugateTriple helixSoft matter
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Collagen overglycosylation: a biochemical feature that may contribute to bone quality.

2005

Skeletal ability to resist mechanical stress is determined by bone amount and quality, which relies on macro- and micro-architecture, turnover, bone matrix, and mineralisation; the role of collagen has not been clearly elucidated. Numerous post-translational steps are involved in collagen type I biosynthesis, including residue hydroxylation and glycosylation catalysed by enzymes that work until the protein folds forming the triple helix; therefore, folding rate regulates these processes. Overglycosylated hydroxylysines are poor substrates for epsilon-amino group deamination which initiates cross-link formation. Three clinical conditions associated with fractures may relate collagen overglyc…

chemistry.chemical_classificationGlycosylationGlycosylationOsteoporosisBiophysicsDeaminationCell BiologyOsteogenesis Imperfectamedicine.diseaseBiochemistryBone and BonesHydroxylationPostmenopausechemistry.chemical_compoundEnzymeBiosynthesischemistryBiochemistryDiabetes Mellitus Type 2Osteogenesis imperfectamedicineHumansCollagenMolecular BiologyTriple helixBiochemical and biophysical research communications
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