2018
Peptides derived from the histidine–proline rich glycoprotein bind copper ions and exhibit anti-angiogenic properties
Magrì A, Grasso G, Corti F, Finetti F, Greco V, Santoro AM, Sciuto S, La Mendola D, Morbidelli L, Rizzarelli E. Peptides derived from the histidine–proline rich glycoprotein bind copper ions and exhibit anti-angiogenic properties. Dalton Transactions 2018, 47: 9492-9503. PMID: 29963662, DOI: 10.1039/c8dt01560k.Peer-Reviewed Original ResearchConceptsElectron paramagnetic resonanceCircular dichroismSpray ionization mass spectrometryPotential drug delivery systemElectron spray ionization mass spectrometryMeans of potentiometryIonization mass spectrometryDrug delivery systemsAmidic bondCopper ionsRole of copperParamagnetic resonanceMass spectrometryComplex speciesTrehalose derivativesProdrug systemEnzymatic degradationDelivery systemCopperPeptidesPotentiometryBondsUVSpectrometryDichroism
2007
Molecular Basis of Branched Peptides Resistance to Enzyme Proteolysis
Falciani C, Lozzi L, Pini A, Corti F, Fabbrini M, Bernini A, Lelli B, Niccolai N, Bracci L. Molecular Basis of Branched Peptides Resistance to Enzyme Proteolysis. Chemical Biology & Drug Design 2007, 69: 216-221. PMID: 17441908, DOI: 10.1111/j.1747-0285.2007.00487.x.Peer-Reviewed Original ResearchConceptsForm of dendrimersDifferent bioactive peptidesStructure-based hypothesesMass spectrometryUnmodified peptidesMultimeric peptidesProteolytic stabilityBioactive peptidesPressure liquid chromatographyLiquid chromatographyHigh-pressure liquid chromatographyLinear moleculesPeptide copiesEnzyme proteolysisProteolytic resistanceHuman plasmaSame peptideSynthetic peptidesPeptidesDendrimersPeptide resistanceSpectrometryMultimericityChromatographyMolecules