Editorial: Formulation and Delivery of Biologics
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RESEARCH PAPER
Editorial: Formulation and Delivery of Biologics Ahmed Besheer 1 & Hanns-Christian Mahler 1
Received: 9 October 2020 / Accepted: 12 October 2020 # Springer Science+Business Media, LLC, part of Springer Nature 2020
KEY WORDS administration . biologics . compatibility . excipients . formulation . parenteral drug product As many new biologics are reaching the market and addressing unmet medical needs, the market for biologics continues to grow, reaching more than 460 Billion US$ by 2023, with a compound annual growth rate of 15% (1). The significant knowledge accumulating over the years has made the development and manufacturing of mAbs become a commodity, while novel biologics with increasing complexity, such as fusion proteins, mAb fragments (2), bispecifics (3), and non-mAb scaffolds (4) are approaching a significant proportion of the R&D pipelines. This increase in structural complexity is associated with increased stability risks and attention to usability, where health authorities are rightfully concerned that the patients get the right dose and quality (5). In addition, there is increasing interest in understanding and simulating the fate of the injected protein product after parenteral administration (6). In this special issue, we compiled various papers that cover many of the rapidly evolving topics for biologics across the value chain. One of the holy grails of protein development is to be able to predict protein stability, and as such select the right mole-
Guest Editors: Ahmed Besheer and Hanns-Christian Mahler * Ahmed Besheer [email protected] * Hanns-Christian Mahler [email protected] 1
Lonza Drug Product Services, Basel, Switzerland
cule candidate for development early on. This is the aim of the developability studies, that look at the molecules’ physicochemical liabilities through a battery of methods and criteria, including in-silico modeling (7), forced degradation studies for chemical degradation (8), and thermodynamic as well as kinetic parameters for physical degradation (9). The later includes evaluating protein self-interaction, which is a measure for a protein’s tendency for aggregation. To this end, Domnowski et al. report on a new method for measuring protein self-interaction using bio-Layer interferometry (BLI) (10). They have evaluated several proteins in a total of 58 formulations, and found out that the new method correlated well with self-interaction coefficient (kD) as obtained by dynamic light scattering, and was useful in ranking the stability of proteins and/or formulations. They also provide a useful comparison of the pros and cons of all seven methods available for measuring protein self-interaction. Meanwhile, Melien et al. evaluated the thermal unfolding as a predictor for protein physical. For this, they measured the apparent melting temperature, by differential scanning calorimetry and differential scanning fluorimetry, as well as the heat of entropy an enthalpy for the different domains of 8 mAbs (11). They found out that the heat of e
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