Document Detail

Water-soluble zinc porphyrins as artificial receptors for amino acids.
MedLine Citation:
PMID:  18827393     Owner:  NLM     Status:  MEDLINE    
The binding of amino acids to water-soluble zinc porphyrins in basic aqueous solution was spectrophotometrically analyzed. The amino acids were bound to the porphyrins through the coordination of the N atom with the central zinc ion. Additional attractions arise due to Coulomb interactions between the -COO(-) anion of the amino acids and the -N(CH(3))(3)(+) cation of the porphyrin substituents and due to hydrophobic interactions between the porphyrin plane and the hydrophobic substituents of the amino acids. These attractions could be explained based on the binding data. The compensatory relationships of DeltaS and DeltaH were also discussed.
Hiroyasu Imai; Kensuke Misawa; Hiroki Munakata; Yoshio Uemori
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Chemical & pharmaceutical bulletin     Volume:  56     ISSN:  0009-2363     ISO Abbreviation:  Chem. Pharm. Bull.     Publication Date:  2008 Oct 
Date Detail:
Created Date:  2008-10-01     Completed Date:  2008-11-14     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0377775     Medline TA:  Chem Pharm Bull (Tokyo)     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  1470-2     Citation Subset:  IM    
Faculty of Pharmaceutical Sciences, Hokuriku University, Kanazawa, Japan.
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MeSH Terms
Amines / chemistry
Magnetic Resonance Spectroscopy
Metalloporphyrins / chemistry*
Receptors, Amino Acid / chemistry*
Reg. No./Substance:
0/Amines; 0/Metalloporphyrins; 0/Receptors, Amino Acid; 13939-11-2/zinc hematoporphyrin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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