A critical measure of the quality of pharmaceutical proteins is the preservation of native conformations of the active pharmaceutical ingredients. Denaturation of the active proteins in any step before administration into patients could lead to loss of potency and/or aggregation, which is associated with an increased risk of immunogenicity of the products. Interfacial stress enhances protein instability as their adsorption to the air-liquid and liquid-solid interfaces are implicated in the formation of denatured proteins and aggregates. While excipients in protein formulations have been employed to reduce the risk of aggregation, the roles of albumin as a stabilizer have not been reviewed from practical and theoretical standpoints. The amphiphilic nature of albumin makes it accumulate at the interfaces. In this review, we aim to bridge the knowledge gap between interfacial instability and the influence of albumin as a surface-active excipient in the context of reducing the immunogenicity risk of protein formulations.
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