The structure, stability, and complex behavior of recombinant human gelatins.

The structure, stability, and complex behavior of recombinant human gelatins. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

The structure, stability, and complex behavior of recombinant human gelatins. Abstract Text:

Nagarajan Thyagarajapuram,David Olsen,C Russell Middaugh,Nagarajan Thyagarajapuram,David Olsen,C Russell Middaugh,Nagarajan Thyagarajapuram,David Olsen,C Russell Middaugh,

Gelatin prepared from animal sources is widely used as a stabilizer in vaccine formulations. The disadvantages associated with their use such as heterogeneity and allerginicity, have led to the development of recombinant human gelatins (rhGs) as a substitute. This study focuses on characterizing the structure and monitoring the physical stability of four molecular weights ( approximately 8.5, 25, 50, and 100 kDa) of rhGs as a function of temperature and pH. The information supplied should be useful in predicting the behavior of rhGs under formulation conditions. A number of spectroscopic techniques were employed in this study. Experimental results indicated that the solution properties of all four rhGs were unpredictable with micro-aggregation observed at various pH values. The 8.5 kDa rhG was found to be in a micro-aggregated state at pH 5 while the 25 kDa rhG was found to be more aggregated at pHs 5, 7, and 8. The properties of these aggregates have been analyzed as a function of temperature. The rhGs were also found to complex with the polyanion heparin through electrostatic and nonelectrostatic interactions. The stability of these complexes has been studied as a function of temperature and pH. (c) 2007 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 96: 3363-3378, 2007.

The structure, stability, and complex behavior of recombinant human gelatins. Publishing Authors By Initials

N Thyagarajapuram,D Olsen,CR Middaugh,N Thyagarajapuram,D Olsen,CR Middaugh,N Thyagarajapuram,D Olsen,CR Middaugh,

For similar abstracts research abstracts see: abstracts research

PUBMED ID PMID:

MEDLINE DATE:

The structure, stability, and complex behavior of recombinant human gelatins. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of pharmaceutical sciences

VOLUME: 96

Page Numbers: 3363-78

Journal Abbreviation:

ISSN: 0022-3549

DAY: 1

MONTH: Dec

YEAR: 2007

The structure, stability, and complex behavior of recombinant human gelatins. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985195

The structure, stability, and complex behavior of recombinant human gelatins. Keywords Mesh Terms:

KEYWORDS:

MESH TERMS:

Chemical & Substance for Abstract: The structure, stability, and complex behavior of recombinant human gelatins. Information

Substance Name:

Registry Number:

Grant and Affiliation Information for The structure, stability, and complex behavior of recombinant human gelatins.

AFFILIATION: Department of Pharmaceutical chemistry, University of Kansas, 2030, Becker Drive, Lawrence, Kansas 66049.

Country: United States

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Pharm Sci

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

The structure, stability, and complex behavior of recombinant human gelatins Related Publications

• A Review of: Vaccine Adjuvants and Delivery Systems.
• A biophysical characterization of the peptide drug pramlintide (AC137) using empirical phase diagrams.
• A network-based analysis of polyanion-binding proteins utilizing human protein arrays.
• A network-based analysis of polyanion-binding proteins utilizing yeast protein arrays.
• A rapid, three-step process for the preformulation of a recombinant ricin toxin A-chain vaccine.
• A systematic approach to stabilizing EBA-175 RII-NG for use as a malaria vaccine.
• Conformational flexibility, hydration and state parameter fluctuations of fibroblast growth factor-10: effects of ligand binding.
• Effects of stabilizers on the destabilization of proteins upon adsorption to aluminum salt adjuvants.
• Immunoglobulin dynamics, conformational fluctuations, and nonlinear elasticity and their effects on stability.
• Intravenous cocaine self-administration: individual differences in male and female C57BL/6J mice.
• Linked outbreaks of hepatitis A in homosexual men and in food service patrons and employees.
• Pandemic influenza preparedness and community resiliency.
• Periadolescent nicotine exposure reduces cocaine reward in adult mice.
• Physical characterization of clostridium difficile toxins and toxoids: effect of the formaldehyde crosslinking on thermal stability.
• Physical stabilization of norwalk virus-like particles.
• Positions of authority may equal lawsuits.
• Preformulation studies of Clostridium difficile toxoids A and B.
• Side effects of diphtheria-tetanus toxoid in adults.
• Spectroscopic methods for the physical characterization and formulation of nonviral gene delivery systems.
• Stabilization of measles virus for vaccine formulation.
• Stabilization of proteins by recombinant human gelatins.
• The analysis of protein pharmaceuticals: near future advances.
• The complex inter-relationships between protein flexibility and stability.
• The interaction of heparin/polyanions with bovine, porcine, and human growth hormone.
• The structure, stability, and complex behavior of recombinant human gelatins.
• pH sensitivity of type III secretion system tip proteins.