title: Characterization of recombinant antibodies for cancer therapy by infrared spectroscopy.
abstract: Fourier transform infrared (FTIR) spectroscopy was used to study the structure of the recombinant antibodies 1E10, anti-CD20 and hR3, which are used as anti-cancer therapeutic drugs. We tested their sensitivity against different conditions and treatments such as pH, temperature, freeze-thaw cycles and drying, which are relevant for the practical usefulness of the drugs. All antibodies were stable against moderate temperature increases (up to 50 °C) and pH changes (range 5-9). 1E10 was sensitive to extreme pH values (pH 3 and 12), whereas hR3 was most sensitive to temperature (at and above 60 °C). We did not observe any significant changes upon freeze-thaw and drying treatments. The secondary structure content of all three antibodies was estimated to be similar to that of IgG with ∼64% β-sheet, 0% α-helix and ∼36% other structure.
authors.affiliation: Center of Molecular Immunology, 216 Street and 15 Avenue, Atabey, Playa, Havana City, Cuba. a.arbesu@yahoo.es
authors.forename: Alejandro Arbesú
authors.initials: AA
authors.lastname: Valdivia
authors.forename: Andreas
authors.initials: A
authors.lastname: Barth
authors.forename: Yamilet Romero
authors.initials: YR
authors.lastname: Batista
authors.forename: Saroj
authors.initials: S
authors.lastname: Kumar
mesh_terms: D000911:Antibodies, Monoclonal / Q000737:chemistry* / Q000235:genetics / Q000627:therapeutic use*; D003890:Desiccation; D004355:Drug Stability; D004356:Drug Storage / Q000379:methods; D005615:Freezing; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009369:Neoplasms / Q000188:drug therapy*; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000627:therapeutic use; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*
chemical_list: D000911:Antibodies, Monoclonal; D011994:Recombinant Proteins