| Calorimetric investigation of protein/amino acid interactions in the solid state. | |
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MedLine Citation:
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PMID: 16427224 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Possible protein/amino acid interactions and the physical states of amino acids after freeze-drying have been studied using isoperibol calorimetry and differential scanning calorimetry (DSC). Good linear correlations (R(2) = 0.99) between the enthalpies of solution and the percentage of antibody in all physical mixtures, as well as unchanging melting temperatures of amino acids for physical mixtures demonstrated that there is no interaction between the antibodies and amino acids studied upon physical mixing. On the other hand, positive deviations for antibody/histidine and antibody/arginine freeze-dried samples obtained from the isoperibol calorimetry results demonstrated that molecular level interactions, such as ion-dipole or electrostatic interactions or hydrogen bonding, occur between antibodies and histidine or arginine. The values of DeltaH(interaction) for antibody/histidine (1:1, w/w) and antibody/arginine (1:1, w/w) lyophilized samples were approximately 8 kJ/mol. These interactions were also confirmed by decreased and/or the disappearance of melting temperatures of the amino acids with DSC measurements. A negative deviation from linearity was detected for antibody/aspartic acid lyophilized samples which indicated partial amorphization of aspartic acid. No deviation from linearity as well as similar melting temperatures of antibody/glycine lyophilized samples indicated the absence of interactions between the antibodies and glycine upon freeze-drying. |
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Authors:
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Fei Tian; Samir Sane; J Howard Rytting |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2006-01-19 |
Journal Detail:
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Title: International journal of pharmaceutics Volume: 310 ISSN: 0378-5173 ISO Abbreviation: Int J Pharm Publication Date: 2006 Mar |
Date Detail:
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Created Date: 2006-02-28 Completed Date: 2006-06-02 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 7804127 Medline TA: Int J Pharm Country: Netherlands |
Other Details:
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Languages: eng Pagination: 175-86 Citation Subset: IM |
Affiliation:
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Department of Pharmaceutical Chemistry, The University of Kansas, 2095 Constant Avenue, Lawrence, KS 66047, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acids
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chemistry* Antibodies / chemistry Arginine / chemistry Aspartic Acid / chemistry Calorimetry, Differential Scanning Circular Dichroism Deoxyribonuclease I / chemistry, genetics Enzyme Stability Freeze Drying Histidine / chemistry Protein Denaturation Proteins / chemistry* Recombinant Proteins / chemistry Solutions Thermodynamics |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 0/Antibodies; 0/Proteins; 0/Recombinant Proteins; 0/Solutions; 56-84-8/Aspartic Acid; 71-00-1/Histidine; 74-79-3/Arginine; EC 3.1.21.1/Deoxyribonuclease I |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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