| Characterization of amorphous solids with weak glass transitions using high ramp rate differential scanning calorimetry. | |
| | |
MedLine Citation:
|
PMID: 17724657 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
Measurement of the glass transition temperature (T(g)) of proteins and other high molecular weight polymers in the amorphous state is often difficult, since the transition is extremely weak, that is, the DeltaC(p) at the glass transition temperature is small. For example, little is known about the solid-state properties of hydroxyethyl starch (HES), which is beginning to become more commonly evaluated as a bulking agent in pharmaceutical products. For weak thermal events, such as the change in heat capacity at the T(g) of a pure protein or large synthetic polymer, increased heating rate should produce greater sensitivity in terms of heat flow. Recent innovations in rapid scanning technology for differential scanning calorimetry (DSC) allow measurements on materials where the thermal events are difficult to detect by conventional DSC. In the current study, measurements of the T(g) of proteins in the solid state, amorphous pharmaceutical excipients which have small DeltaC(p) at the glass transition temperature, and bacterial spores, have all been made using high ramp rate DSC, providing information on materials that was inaccessible using conventional DSC methods. |
| | |
Authors:
|
Derrick S Katayama; John F Carpenter; Mark Cornell Manning; Theodore W Randolph; Peter Setlow; Kevin P Menard |
Related Documents
:
|
15783597 - Domain-enhanced interlayer coupling in ferroelectric/paraelectric superlattices. 2421777 - The microsecond rotational motions of eosin-labelled fatty acids in multilamellar vesic... 3801567 - The influence of cholesterol on the main phase transition of unilamellar dipalmytoylpho... 22418357 - Silicon photodiodes with high photoconductive gain at room temperature. 19614667 - Ubiquitination of the bacterial inositol phosphatase, sopb, regulates its biological ac... 718847 - Organization of rhodopsin in photoreceptor membranes. 2. transmembrane organization of ... |
Publication Detail:
|
Type: Journal Article |
Journal Detail:
|
Title: Journal of pharmaceutical sciences Volume: 97 ISSN: 0022-3549 ISO Abbreviation: J Pharm Sci Publication Date: 2008 Feb |
Date Detail:
|
Created Date: 2007-12-27 Completed Date: 2008-04-03 Revised Date: - |
Medline Journal Info:
|
Nlm Unique ID: 2985195R Medline TA: J Pharm Sci Country: United States |
Other Details:
|
Languages: eng Pagination: 1013-24 Citation Subset: IM |
Affiliation:
|
Department of Pharmaceutical Sciences, Center for Pharmaceutical Biotechnology, University of Colorado Health Sciences Center, Denver, Colorado, USA. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Calorimetry, Differential Scanning
/
methods* Freeze Drying Hetastarch / chemistry Proteins / chemistry* Spores, Bacterial / physiology |
| Chemical | |
Reg. No./Substance:
|
0/Proteins; 9005-27-0/Hetastarch |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Mucoadhesive tablet releasing iodine for treating oral infections.
Next Document: Biorelevant refinement of the Caco-2 cell culture model to assess efficacy of paracellular permeabil...