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ROW regulatory guidance
Published in Sarfaraz K. Niazi, Biosimilars and Interchangeable Biologics, 2016
Current technologies, such as peptide mapping, protein sequencing, and mass spectroscopy enable manufacturers to determine, with certainty, the amino acid sequence of a recombinant protein. However, the amino acid sequence is the most rudimentary characteristic of a protein. Conclusive analysis of other aspects of a protein’s structure requires much more sophisticated technologies and is fraught with uncertainties that are proportional to the size and complexity of the protein itself. Therefore, the ability to predict the clinical comparability of two products depends on our understanding of the relationship between the structural characteristics of the protein and its function, as well as on our ability to demonstrate structural similarity between the biosimilar product and the reference product. Although this may be currently possible for some relatively simple protein products, technology is not yet sufficiently advanced to allow this type of comparison for more complex protein products. Similarity will therefore need to be confirmed via nonclinical and clinical studies.
Catalytic valorization of raw glycerol derived from biodiesel: a review
Published in Biofuels, 2018
Sravanthi Veluturla, Narula Archna, D. Subba Rao, N. Hezil, I.S. Indraja, S. Spoorthi
A new process, fast-atom bombardment-induced condensation (FAB) of glycerol with ammonium surfactants I [60] and ammonium surfactants II [61] was studied. This new process basically was used for protein sequencing which was found to be effective for condensations reactions also. Mauro Marzi et al. [62] successfully described a process of synthesis of R-(−)-carnitine by condensation of glycerol with an amine of camphorsulfonic acid. This process was found to be economical as the conventional processes practiced in the industries had major drawbacks which included low yield and expensive nutrient media for micro-organism culture. This invention was successful in giving a stereo selective synthesis without any resolution of racemic mixtures and precursors.
Probing radical versus proton migration in the aniline cation with IRMPD spectroscopy
Published in Molecular Physics, 2023
Laura Finazzi, Jonathan Martens, Giel Berden, Jos Oomens
In contrast, collision-induced dissociation (CID) of closed-shell protonated species formed in electrospray ionisation (ESI) has been shown to be driven predominantly by proton transfer processes. The dissociation mechanisms of protonated peptides have been especially well studied in this regard in attempts to gain insight into the mechanistics underlying MS-based peptide and protein sequencing. Indeed, the “mobile proton model” of peptide dissociation [14–17] emphasises the role of proton transfer in these mechanisms. Note that efforts to understand ExD dissociation mechanisms have also focussed particularly on peptides because of the use of ExD in protein sequencing applications.