Source:http://linkedlifedata.com/resource/pubmed/id/16117548
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
34
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pubmed:dateCreated |
2005-8-24
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pubmed:abstractText |
Various amino acid-carrying amphiphiles were synthesized, and the pK values of the attached amino acid residues were investigated at the air-water interface and in aqueous vesicles using pi-A isotherm measurements, (1)H NMR titration, and IR spectroscopy in reflection-adsorption mode. The epsilon-amino group of the Lys residue embedded at the air-water interface displays a significant pK shift (4 or 5 unit) compared with that observed in bulk water, while the pK shift in aqueous vesicles was not prominent (ca. 1 unit). Moreover, pK values of the amino acids at the air-water interface can be tuned simply by control of the subphase ionic strength as well as by molecular design of the amphiphiles. A simple equation based on the dominant contribution by the electrostatic energy to the pK shift reproduces well the surface pressure difference between protonated and unprotonated species, suggesting a reduction in the apparent dielectric constant at the air-water interface. Hydrolysis of a p-nitrophenyl ester derivative was used as a model reaction to demonstrate the use of the Lys-functionalized monolayer. Efficient hydrolysis was observed, even at neutral pH, after tuning of pK for the Lys residue in the monolayer, which is a similar case to that occurring in biological catalysis.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Esters,
http://linkedlifedata.com/resource/pubmed/chemical/Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrophenols,
http://linkedlifedata.com/resource/pubmed/chemical/Water
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0002-7863
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
127
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12074-80
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:16117548-Air,
pubmed-meshheading:16117548-Amino Acids,
pubmed-meshheading:16117548-Catalysis,
pubmed-meshheading:16117548-Enzymes,
pubmed-meshheading:16117548-Esters,
pubmed-meshheading:16117548-Hydrogen-Ion Concentration,
pubmed-meshheading:16117548-Hydrolysis,
pubmed-meshheading:16117548-Lipids,
pubmed-meshheading:16117548-Magnetic Resonance Spectroscopy,
pubmed-meshheading:16117548-Nitrophenols,
pubmed-meshheading:16117548-Osmolar Concentration,
pubmed-meshheading:16117548-Spectrophotometry, Infrared,
pubmed-meshheading:16117548-Static Electricity,
pubmed-meshheading:16117548-Surface Properties,
pubmed-meshheading:16117548-Thermodynamics,
pubmed-meshheading:16117548-Water
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pubmed:year |
2005
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pubmed:articleTitle |
Tunable pK of amino acid residues at the air-water interface gives an L-zyme (langmuir enzyme).
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pubmed:affiliation |
Supermolecules Group, Advanced Materials Laboratory, National Institute for Materials Science (NINS), 1-1 Namiki, Tsukuba 305-0044, Japan. ARIGA.Katsuhiko@nims.go.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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