Literature DB >> 24859390

Storage stability of keratinocyte growth factor-2 in lyophilized formulations: effects of formulation physical properties and protein fraction at the solid-air interface.

Dilip Devineni1, Christoph Gonschorek2, Marcus T Cicerone3, Yemin Xu4, John F Carpenter1, Theodore W Randolph5.   

Abstract

Lyophilized formulations of keratinocyte growth factor-2 (KGF-2) were prepared with a range of disaccharide (sucrose or trehalose) and hydroxyethyl starch (HES) mass ratios. Protein degradation was assessed as a function of time of storage of the dried formulations at 40, 50 and 60°C. Lyophilized and stored samples were rehydrated, and protein degradation was quantified by measuring loss of monomeric protein with size exclusion chromatography and by determining chemical degradation in the soluble fraction with reverse-phase chromatography. The secondary structure of the protein in the lyophilized formulations was studied with infrared spectroscopy. The magnitudes of degradation were compared the key physical properties of the formulations including retention of protein native secondary structure, glass transition temperature (Tg), inverse mean square displacements 〈u(2)〉(-1) for hydrogen atoms (fast β relaxation), and the relaxation time τ(β), which correlates with relaxation due to fast Johari-Goldstein motions in the glass (Xu et al., 2013) [1]. In addition, specific surface areas of the lyophilized formulations were determined by Brunauer-Emmet-Teller analysis of krypton adsorption isotherms and used to estimate the fraction of the KGF-2 molecules residing at the solid-air interface. KGF-2 degradation rates were highest in formulations wherein the protein's structure was most perturbed, and wherein β relaxations were fastest, but the dominant factor governing KGF-2 degradation in freeze-dried formulations was the fraction of the protein found at the glass solid-air interface.
Copyright © 2014 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Glass dynamics; Glass transition temperature; Global mobility; KGF-2; Local mobility; Lyophilization; Protein interfacial adsorption; Protein stability; Protein structure; Structural relaxation time

Mesh:

Substances:

Year:  2014        PMID: 24859390      PMCID: PMC4240752          DOI: 10.1016/j.ejpb.2014.05.012

Source DB:  PubMed          Journal:  Eur J Pharm Biopharm        ISSN: 0939-6411            Impact factor:   5.571


  33 in total

1.  Comparability of protein therapeutics: quantitative comparison of second-derivative amide I infrared spectra.

Authors:  Jennifer D'antonio; Brian M Murphy; Mark Cornell Manning; Wasfi A Al-Azzam
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2.  Drying-induced variations in physico-chemical properties of amorphous pharmaceuticals and their impact on Stability II: stability of a vaccine.

Authors:  Ahmad M Abdul-Fattah; Vu Truong-Le; Luisa Yee; Emilie Pan; Yi Ao; Devendra S Kalonia; Michael J Pikal
Journal:  Pharm Res       Date:  2007-02-15       Impact factor: 4.200

3.  beta-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1 beta and 1 alpha and fibroblast growth factors.

Authors:  A G Murzin; A M Lesk; C Chothia
Journal:  J Mol Biol       Date:  1992-01-20       Impact factor: 5.469

4.  Kinetics of insulin aggregation in aqueous solutions upon agitation in the presence of hydrophobic surfaces.

Authors:  V Sluzky; J A Tamada; A M Klibanov; R Langer
Journal:  Proc Natl Acad Sci U S A       Date:  1991-11-01       Impact factor: 11.205

5.  Evidence of partial unfolding of proteins at the ice/freeze-concentrate interface by infrared microscopy.

Authors:  J Jeff Schwegman; John F Carpenter; Steven L Nail
Journal:  J Pharm Sci       Date:  2009-09       Impact factor: 3.534

Review 6.  Effects of surfaces and leachables on the stability of biopharmaceuticals.

Authors:  Jared S Bee; Theodore W Randolph; John F Carpenter; Steven M Bishop; Mariana N Dimitrova
Journal:  J Pharm Sci       Date:  2011-04-26       Impact factor: 3.534

7.  Surface-induced denaturation of proteins during freezing and its inhibition by surfactants.

Authors:  B S Chang; B S Kendrick; J F Carpenter
Journal:  J Pharm Sci       Date:  1996-12       Impact factor: 3.534

8.  Hydrogen bonding between sugar and protein is responsible for inhibition of dehydration-induced protein unfolding.

Authors:  S D Allison; B Chang; T W Randolph; J F Carpenter
Journal:  Arch Biochem Biophys       Date:  1999-05-15       Impact factor: 4.013

9.  Effects of Tween 80 and sucrose on acute short-term stability and long-term storage at -20 degrees C of a recombinant hemoglobin.

Authors:  B A Kerwin; M C Heller; S H Levin; T W Randolph
Journal:  J Pharm Sci       Date:  1998-09       Impact factor: 3.534

10.  Characterization of dynamics in complex lyophilized formulations: I. Comparison of relaxation times measured by isothermal calorimetry with data estimated from the width of the glass transition temperature region.

Authors:  Norman Chieng; Masayasu Mizuno; Michael Pikal
Journal:  Eur J Pharm Biopharm       Date:  2013-04-20       Impact factor: 5.571

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  4 in total

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Authors:  Marcus T Cicerone; Michael J Pikal; Ken K Qian
Journal:  Adv Drug Deliv Rev       Date:  2015-05-14       Impact factor: 15.470

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4.  Characterization and Dissolution Study of Micellar Curcumin-Spray Dried Powder for Oral Delivery.

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  4 in total

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