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Basics of Sterile Compounding: Manipulating Peptides and Proteins
1Baxter BioPharma Solutions, Bloomington, Indiana. mjakers356@gmail.com.
International Journal of Pharmaceutical Compounding
|May 31, 2017
Summary
Biopharmaceutical stability is often compromised by tertiary structure. This article briefly outlines strategies to minimize physical and chemical stability issues associated with protein structure.
Area of Science:
- Biopharmaceutical science
- Protein chemistry
- Drug stability
Background:
- Biopharmaceuticals possess primary, secondary, and tertiary structures.
- Tertiary structure presents significant challenges to biopharmaceutical stability.
- Physical and chemical degradation pathways are often linked to protein folding.
Purpose of the Study:
- To identify and briefly discuss common stability issues in biopharmaceuticals.
- To provide an overview of strategies for minimizing stability problems.
- To highlight the importance of understanding tertiary structure for formulation development.
Main Methods:
- Literature review of biopharmaceutical stability studies.
- Analysis of common degradation mechanisms related to protein structure.
- Summary of formulation and processing approaches to enhance stability.
Main Results:
- Tertiary structure is a critical determinant of both physical and chemical stability.
- Specific formulation excipients and processing conditions can mitigate degradation.
- Understanding protein aggregation and denaturation is key to maintaining drug efficacy.
Conclusions:
- Minimizing stability issues in biopharmaceuticals requires a focus on tertiary structure.
- Proactive strategies in formulation and manufacturing are essential for product longevity.
- Further research into structure-stability relationships will advance biopharmaceutical development.
