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Physicochemical Characteristics of Transferon™ Batches. | LitMetric

Physicochemical Characteristics of Transferon™ Batches.

Biomed Res Int

Unidad de Desarrollo e Investigación en Bioprocesos (UDIBI), Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Prolongación de Carpio y Plan de Ayala s/n, Colonia Santo Tomás, 11340 Ciudad de México, Mexico; Departamento de Inmunología, Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Prolongación de Carpio y Plan de Ayala s/n, Colonia Santo Tomás, 11340 Ciudad de México, Mexico; Unidad de Investigación, Desarrollo e Innovación Médica y Biotecnológica (UDIMEB), Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Prolongación de Carpio y Plan de Ayala s/n, Colonia Santo Tomás, 11340 Ciudad de México, Mexico.

Published: February 2017

AI Article Synopsis

  • Transferon, a biotherapeutic agent used for inflammatory diseases, has recently been approved in Mexico for treating herpes infections.
  • Its active ingredient consists of peptides derived from human leukocytes, processed through dialysis and ultrafiltration, specifically targeting molecules under 10 kDa.
  • Various analytical methods confirmed consistent batch composition and identified glycine as the most prevalent amino acid, with mass spectrometry helping establish Transferon's unique peptide identity.

Article Abstract

Transferon, a biotherapeutic agent that has been used for the past 2 decades for diseases with an inflammatory component, has been approved by regulatory authorities in Mexico (COFEPRIS) for the treatment of patients with herpes infection. The active pharmaceutical ingredient (API) of Transferon is based on polydispersion of peptides that have been extracted from lysed human leukocytes by a dialysis process and a subsequent ultrafiltration step to select molecules below 10 kDa. To physicochemically characterize the drug product, we developed chromatographic methods and an SDS-PAGE approach to analyze the composition and the overall variability of Transferon. Reversed-phase chromatographic profiles of peptide populations demonstrated batch-to-batch consistency from 10 representative batches that harbored 4 primary peaks with a relative standard deviation (RSD) of less than 7%. Aminogram profiles exhibited 17 proteinogenic amino acids and showed that glycine was the most abundant amino acid, with a relative content of approximately 18%. Further, based on their electrophoretic migration, the peptide populations exhibited a molecular mass of about 10 kDa. Finally, we determined the Transferon fingerprint using a mass spectrometry tool. Because each batch was produced from independent pooled buffy coat samples from healthy donors, supplied by a local blood bank, our results support the consistency of the production of Transferon and reveal its peptide identity with regard to its physicochemical attributes.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4971316PMC
http://dx.doi.org/10.1155/2016/7935181DOI Listing

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