Journal Article10.1002/JPS.2600840407
Infrared Spectroscopic Studies of Lyophilization‐ and Temperature‐Induced Protein Aggregation
TL;DR: The purpose of the current review is to provide an overview of these topics, as well as an introduction to the study of protein secondary structure with IR spectroscopy.
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About: This article is published in Journal of Pharmaceutical Sciences. The article was published on 01 Apr 1995. The article focuses on the topics: Protein stabilization.
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Citations
Lyophilization and development of solid protein pharmaceuticals
TL;DR: Four interrelated topics are discussed: lyophilization and its denaturation stresses, cryo- and lyo-protection of proteins by excipients, design of a robust lyophILization cycle, and with emphasis, instability, stabilization, and formulation of solid protein pharmaceuticals.
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Physical Stability of Proteins in Aqueous Solution: Mechanism and Driving Forces in Nonnative Protein Aggregation
TL;DR: The purpose of the current review is to provide a fundamental understanding of the mechanisms by which proteins aggregate and by which varying solution conditions, such as temperature, pH, salt type, salt concentration, cosolutes, preservatives, and surfactants, affect this process.
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The role of vitrification in anhydrobiosis.
TL;DR: Evidence is presented here showing that trehalose has a remarkably high glass-transition temperature (Tg), which makes this sugar useful in stabilization of biomolecules of use in human welfare and may explain the stability and longevity of anhydrobiotes that contain it.
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Instability, stabilization, and formulation of liquid protein pharmaceuticals.
TL;DR: The basic behavior of proteins, their instabilities, and stabilization in aqueous state in relation to the development of liquid protein pharmaceuticals is discussed.
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Protein aggregation: folding aggregates, inclusion bodies and amyloid
TL;DR: Substantial data support the hypothesis that partially folded intermediates are key precursors to aggregates, that aggregation involves specific intermolecular interactions and that most aggregates involve beta sheets.
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References
Examination of the secondary structure of proteins by deconvolved FTIR spectra.
D M Byler,H. Susi +1 more
TL;DR: Fourier transform ir (FTIR) spectra of 21 globular proteins have been obtained, revealing that the amide I band of each protein except casein consists of six to nine components, although all proteins do not exhibit components at every characteristic frequency.
2.9K
Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins.
Samuel Krimm,Jagdeesh Bandekar +1 more
TL;DR: The aim of this chapter is to present recent developments in the vibrational spectroscopy of peptides, polypeptides, and proteins.
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Structure and stability of biological macromolecules
Serge N. Timasheff,Gerald D. Fasman +1 more
- 01 Jan 1969
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