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Identity profiling of complex mixtures of peptide products by structural and mass mobility orthogonal analysis

dc.creatorVázquez-Leyva, Saides_ES
dc.creatorVallejo-Castillo, Luises_ES
dc.creatorLópez-Morales, Carlos A.es_ES
dc.creatorHerbert-Pucheta, José Enriquees_ES
dc.creatorZepeda-Vallejo, L. Gerardoes_ES
dc.creatorVelasco-Velázquez, Marcoes_ES
dc.creatorPavón, Lenines_ES
dc.creatorPérez-Tapia, Sonia M.es_ES
dc.creatorMedina-Rivero, Emilioes_ES
dc.date2019
dc.date.accessioned2021-06-15T17:52:23Z
dc.date.available2021-06-15T17:52:23Z
dc.date.issued2019es_ES
dc.identifierJC003es_ES
dc.identifier.issn0003-2700es_ES
dc.identifier.urihttp://repositorio.inprf.gob.mx/handle/123456789/7461
dc.identifier.urihttps://doi.org/10.1021/acs.analchem.9b02873
dc.descriptionIdentity is a critical quality attribute that must be determined before releasing batches of medicinal and dietary products. However, the identities of peptide-derived products composed of a large number of diverse molecules is challenging since most analytical techniques cannot analyze multiple molecules simultaneously. Here, we proposed the determination of the weight-average molecular weight (Mw) and polydispersity index (PDI) by mass spectrometry for control quality for the batch release of complex products, namely, glatiramer acetate (Copaxone), collagen hydrolysate (Colagenart), and a human dialyzable leucocyte extract (Transferon). The Mw and PDI values were orthogonally determined by PFG-STE-H2O(presaturation)-DOSY-NMR analysis. To the best of our knowledge, this is the first time that MS and NMR spectra have been combined to determine the PDI of complex products derived from protein hydrolysis that are not monodisperse. The performance of each method was evaluated by comparing the obtained results to those reported for glatiramer acetate using MALLS, the technique commonly employed to determine PDI. This combined approach demonstrates the ability of these techniques to separate peptide populations from complex mixtures to establish their identity through their mass distribution profiles.es_ES
dc.formatAdobe PDFes_ES
dc.language.isoenges_ES
dc.publisherACS Publicationses_ES
dc.relation91(22) 14392-14400 p.
dc.relationversión del editores_ES
dc.rightsacceso cerradoes_ES
dc.sourceAnalytical Chemistry Vol. 91 no. 22 p. 14392-14400 (2019)es_ES
dc.subject.meshCollagen / chemistry*
dc.subject.meshGlatiramer Acetate / chemistry*
dc.subject.meshHumans
dc.subject.meshHydrolysis
dc.subject.meshImmunosuppressive Agents / chemistry*
dc.subject.meshLeukocytes / chemistry*
dc.subject.meshMagnetic Resonance Spectroscopy / methods
dc.subject.meshMass Spectrometry / methods*
dc.subject.meshMolecular Weight
dc.titleIdentity profiling of complex mixtures of peptide products by structural and mass mobility orthogonal analysises_ES
dc.typeArtículoes_ES
dc.contributor.affiliationUnidad de Desarrollo e Investigación en Bioprocesos (UDIBI), Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional. 11340 Mexico City, Méxicoes_ES
dc.contributor.emailemilio.medina@udibi.com.mxes_ES
dc.relation.jnabreviadoANAL CHEMes_ES
dc.relation.journalAnalytical Chemistry
dc.identifier.placeEstados Unidoses_ES
dc.date.published2019es_ES
dc.identifier.organizacionInstituto Nacional de Psiquiatría Ramón de la Fuente Muñizes_ES
dc.identifier.eissn1520-6882es_ES
dc.identifier.doi10.1021/acs.analchem.9b02873


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