Screening for stability and compatibility conditions of recombinant human epidermal growth factor for parenteral formulation: Effect of pH, buffers, and excipients

Evaluation of etanercept degradation under oxidative stress and potential protective effects of various amino acids

“…SEC can detect various types of aggregation and fragmentation, which is a major concern because of the product purity and immunogenicity issues (Maarschalkerweerd et al, 2011;Manikwar et al, 2013;Santana et al, 2013). In the present study, under accelerated temperature conditions, the content of monomers and aggregates decreases but the fragments increase upon oxidation (Table 2 and 3, Fig.…”

EGF Functionalized Polymer-Coated Gold Nanoparticles Promote EGF Photostability and EGFR Internalization for Photothermal Therapy

“…The native structure of EGF is described to be mainly composed of random coil elements (72%) and β-helical elements (25%) and only a trace of α-helical content [3]. The random coil secondary structure contributes to the presence of a negative peak at 200–210 nm [54]. Although a typical shoulder formation at 220 nm is described for EGF [54], as indicative of the presence of random non-helical forms and β-sheets, spectra with a flat curve around 215–225 nm is also expected for EGF, suggesting a low content on β forms [55].…”

“…The random coil secondary structure contributes to the presence of a negative peak at 200–210 nm [54]. Although a typical shoulder formation at 220 nm is described for EGF [54], as indicative of the presence of random non-helical forms and β-sheets, spectra with a flat curve around 215–225 nm is also expected for EGF, suggesting a low content on β forms [55]. It has been observed this flat curvature for all spectra of EGF samples above 215–220 nm (Fig 12).…”

Solid-State mAbs and ADCs Subjected to Heat-Stress Stability Conditions can be Covalently Modified with Buffer and Excipient Molecules

“…[10][11][12] Deamidation of Asn residues and cyclic imide/isomerization occurring on Asp residues are common degradation events that are observed on proteins regardless of the physical state. [13][14][15][16][17][18] The rate of chemical modification on Asn and Asp residues varies widely and depends on the pH and cosolvents in the formulation buffer, [19][20][21][22][23] the position and solvent accessibility of the residue, 24 and the storage and stress conditions. 25,26 Controlling oxidation levels on Met and Trp residues is also important for ensuring biotherapeutic integrity.…”