Biothermodynamic characterization of monocarboxylic and dicarboxylic aliphatic acids binding to human serum albumin: A flow microcalorimetric study
Identifieur interne : 003184 ( Main/Merge ); précédent : 003183; suivant : 003185Biothermodynamic characterization of monocarboxylic and dicarboxylic aliphatic acids binding to human serum albumin: A flow microcalorimetric study
Auteurs : Hatsumi Aki [Japon] ; Magobei Yamamoto [Japon]Source :
- Biophysical Chemistry [ 0301-4622 ] ; 1992.
Abstract
Thermodynamic parameters have been evaluated for the binding of unbranched monocarboyxlic aliphatic acids (MCAs) of 4 to 16 carbons (MC4 to MC16) and dicarboxylic aliphatic acids (DCAs) of 4 to 16 carbons (DC4 to DC16) to human serum albumin (HSA) on the basis of microcalorimetric measurement at pH 7.4 and 37°C by computer-fitting to single- and two-class binding models. Long-chain MCAs (MC10 to MC16) and DCAs (DC14 and DC16) had the first class of binding sites with high affinity (large binding constant) of 105 to 10∂ M−1 and the second class with lower affinity and high capacity (large numbers of binding sites). Short- or medium-chain MCAs and DCAs bound to HSA at some low affinity binding sites. The binding constants of MCAs were ten times larger than those of DCAS. All the relationships between the thermodynamic parameters and alkyl-chain length of the acids showed clear-cut inflections in their plots around eight or nine methylene units. The free energy change of the first class of binding sites (-Δ1) became more negative with an increment of −1.0 kJ mo1−1 CH−12 as the alkyl-chain length increased, but there were steep rises between MC9 and MC11 with −2.90 kJ mo1−1 CH−12 and between DC9 and DC12 with −2.02 kJ mo1−1 CH2−1. The enthalpy change (−ΔH) increased at the rate of −7.4 kJ mo1−1 CH2−1to the maximum at MC9 and DC10, then decreased due to hydrophobicity of the alkyl-chains. From compensation analyses (ΔH vs. ΔS and ΔG), HSA binding sites were characterized into three groups.
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DOI: 10.1016/0301-4622(93)87010-T
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<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>Biothermodynamic characterization of monocarboxylic and dicarboxylic aliphatic acids binding to human serum albumin: A flow microcalorimetric study</title><author><name sortKey="Aki, Hatsumi" sort="Aki, Hatsumi" uniqKey="Aki H" first="Hatsumi" last="Aki">Hatsumi Aki</name></author><author><name sortKey="Yamamoto, Magobei" sort="Yamamoto, Magobei" uniqKey="Yamamoto M" first="Magobei" last="Yamamoto">Magobei Yamamoto</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:880D6C8D188EDF005AB04BBF601ABF0267C0ED83</idno><date when="1993" year="1993">1993</date><idno type="doi">10.1016/0301-4622(93)87010-T</idno><idno type="url">https://api.istex.fr/document/880D6C8D188EDF005AB04BBF601ABF0267C0ED83/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">002613</idno><idno type="wicri:Area/Istex/Curation">002442</idno><idno type="wicri:Area/Istex/Checkpoint">002273</idno><idno type="wicri:doubleKey">0301-4622:1993:Aki H:biothermodynamic:characterization:of</idno><idno type="wicri:Area/Main/Merge">003184</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">Biothermodynamic characterization of monocarboxylic and dicarboxylic aliphatic acids binding to human serum albumin: A flow microcalorimetric study</title><author><name sortKey="Aki, Hatsumi" sort="Aki, Hatsumi" uniqKey="Aki H" first="Hatsumi" last="Aki">Hatsumi Aki</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Pharmaceutics, Faculty of Pharmaceutical Sciences, Fukuoka University, 8-19-1 Nanakuma, Jonan-ku</wicri:regionArea><wicri:noRegion>Jonan-ku</wicri:noRegion></affiliation></author><author><name sortKey="Yamamoto, Magobei" sort="Yamamoto, Magobei" uniqKey="Yamamoto M" first="Magobei" last="Yamamoto">Magobei Yamamoto</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Pharmaceutics, Faculty of Pharmaceutical Sciences, Fukuoka University, 8-19-1 Nanakuma, Jonan-ku</wicri:regionArea><wicri:noRegion>Jonan-ku</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Biophysical Chemistry</title><title level="j" type="abbrev">BIOCHE</title><idno type="ISSN">0301-4622</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1992">1992</date><biblScope unit="volume">46</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="91">91</biblScope><biblScope unit="page" to="99">99</biblScope></imprint><idno type="ISSN">0301-4622</idno></series><idno type="istex">880D6C8D188EDF005AB04BBF601ABF0267C0ED83</idno><idno type="DOI">10.1016/0301-4622(93)87010-T</idno><idno type="PII">0301-4622(93)87010-T</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0301-4622</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thermodynamic parameters have been evaluated for the binding of unbranched monocarboyxlic aliphatic acids (MCAs) of 4 to 16 carbons (MC4 to MC16) and dicarboxylic aliphatic acids (DCAs) of 4 to 16 carbons (DC4 to DC16) to human serum albumin (HSA) on the basis of microcalorimetric measurement at pH 7.4 and 37°C by computer-fitting to single- and two-class binding models. Long-chain MCAs (MC10 to MC16) and DCAs (DC14 and DC16) had the first class of binding sites with high affinity (large binding constant) of 105 to 10∂ M−1 and the second class with lower affinity and high capacity (large numbers of binding sites). Short- or medium-chain MCAs and DCAs bound to HSA at some low affinity binding sites. The binding constants of MCAs were ten times larger than those of DCAS. All the relationships between the thermodynamic parameters and alkyl-chain length of the acids showed clear-cut inflections in their plots around eight or nine methylene units. The free energy change of the first class of binding sites (-Δ1) became more negative with an increment of −1.0 kJ mo1−1 CH−12 as the alkyl-chain length increased, but there were steep rises between MC9 and MC11 with −2.90 kJ mo1−1 CH−12 and between DC9 and DC12 with −2.02 kJ mo1−1 CH2−1. The enthalpy change (−ΔH) increased at the rate of −7.4 kJ mo1−1 CH2−1to the maximum at MC9 and DC10, then decreased due to hydrophobicity of the alkyl-chains. From compensation analyses (ΔH vs. ΔS and ΔG), HSA binding sites were characterized into three groups.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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