Document Detail


Calorimetric investigation of protein/amino acid interactions in the solid state.
MedLine Citation:
PMID:  16427224     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Fei Tian; Samir Sane; J Howard Rytting
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-01-19
Journal Detail:
Title:  International journal of pharmaceutics     Volume:  310     ISSN:  0378-5173     ISO Abbreviation:  Int J Pharm     Publication Date:  2006 Mar 
Date Detail:
Created Date:  2006-02-28     Completed Date:  2006-06-02     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  7804127     Medline TA:  Int J Pharm     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  175-86     Citation Subset:  IM    
Affiliation:
Department of Pharmaceutical Chemistry, The University of Kansas, 2095 Constant Avenue, Lawrence, KS 66047, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / 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:
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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