Journal ArticleDOI
Instability, stabilization, and formulation of liquid protein pharmaceuticals.
TLDR
The basic behavior of proteins, their instabilities, and stabilization in aqueous state in relation to the development of liquid protein pharmaceuticals is discussed.About:
This article is published in International Journal of Pharmaceutics.The article was published on 1999-08-20. It has received 1288 citations till now.read more
Citations
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Journal ArticleDOI
Polyionic hydrocolloids for the intestinal delivery of protein drugs: alginate and chitosan--a review.
Meera George,T. Emilia Abraham +1 more
TL;DR: Alginate, being an anionic polymer with carboxyl end groups, is a good mucoadhesive agent and cross-linked alginate has more capacity to retain the entrapped drugs and mixing of alginates with other polymers such as neutral gums, chitosan, and eudragit have been found to solve the problem of drug leaching.
Journal ArticleDOI
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.
Journal ArticleDOI
Effects of protein aggregates: an immunologic perspective.
TL;DR: Protein antigens presented in a highly arrayed structure, such as might be found in large nondenatured aggregate species, are highly potent in inducing antibody responses even in the absence of T-cell help.
Journal ArticleDOI
Antibody structure, instability, and formulation
TL;DR: The structure and function of antibodies and the mechanisms of physical and chemical instabilities are reviewed and various aspects of formulation development have been examined to identify the critical attributes for the stabilization of antibodies.
Journal ArticleDOI
Protein drug stability: a formulation challenge
Sven Frokjaer,Daniel E. Otzen +1 more
TL;DR: The increasing use of recombinantly expressed therapeutic proteins in the pharmaceutical industry has highlighted issues such as their stability during long-term storage and means of efficacious delivery that avoid adverse immunogenic side effects as discussed by the authors.
References
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Journal ArticleDOI
Dominant forces in protein folding
TL;DR: The present review aims to provide a reassessment of the factors important for folding in light of current knowledge, including contributions to the free energy of folding arising from electrostatics, hydrogen-bonding and van der Waals interactions, intrinsic propensities, and hydrophobic interactions.
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Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment.
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Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
TL;DR: Results of these studies indicate that the most common pathway for the oxidation of simple aliphatic amino acids involves the hydroxyl radical-mediated abstraction of a hydrogen atom to form a carbon-centered radical at the alpha-position of the amino acid or amino acid residue in the polypeptide chain.
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Stability of Protein Pharmaceuticals
TL;DR: Current methodology to stabilize proteins is presented, including additives, excipients, chemical modification, and the use of site-directed mutagenesis to produce a more stable protein species.
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Protein secondary structures in water from second-derivative amide I infrared spectra.
TL;DR: A method of analysis of second-derivative amide I spectra whereby the frequencies of bands due to different secondary structures can be obtained is demonstrated and the band intensities obtained provide a useful method for estimating the relative amounts of different structures.