Interaction of 3'-0-caffeoyal D-quinic acid with human serum albumin.
IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore
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http://ir.cftri.com/4486/
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| Title |
Interaction of 3'-0-caffeoyal D-quinic acid with human serum albumin.
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| Creator |
Muralidhara, B. K.
Prakash, V. |
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| Subject |
09 Human Physiology
03 Proteins |
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| Description |
The interaction of chlorogenic acid (CGA) with human serum albumin (HSA) was studied from the viewpoint
of thermodynamics and mechanism of binding at pH 6.0. The association constants (K,) for the
HSA-CGA interaction at 10, 25 and 40 "C were 6.0 X lo4, 9.0 x lo3 and 2 x lo4 M- I , resulting in AG of
-6.21, -5.80, -6.32 kcal/niol, respectively. These high &-values showed that the interaction between CGA
and HSA is strong, endothermic and entropically driven. Binding of chlorogenic acid induces conformational
change in HSA as indicated by quenching of fluorescence emission intensity along with a red shift in the
emission maxima from 338 LO 350 nm. This suggested the involvement of the lone tryptophan residue in the
region of binding. Far-ultraviolet circular dichroic data showed a decrease in the a-helical content of HSA
from 56 to 50% upon binding of CGA. These data are also supported by the decrease in the apparent T,
of HSA by 4 "C upon binding of CGA causing destabilization of the HSA molecule. The kinetics of the
interaction involves a single step in the binding, and the kinetic curve attains equilibrium within 180 5 s. Data
on caffeic acid (CA) and quinic acid (QA), which are the hydrolysis products of the bidentate CGA molecule,
indicate that CA interacts more strongly than CGA. CA binds with an association constant of 8 x lo4 M -
and with a maximum number of binding sites of four. Microcalorimetric investigation of the interaction of
these ligands with HSA suggests that the strength of binding follows the order CA>> CGA>>> QA with a
single class of binding sites. The effect of temperature on the binding of CGA to HSA showed that the interaction
is dominated by hydrophobic forces and hydrogen bonding.
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| Date |
1995
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| Type |
Article
PeerReviewed |
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| Format |
pdf
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| Language |
en
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| Identifier |
http://ir.cftri.com/4486/1/International%20Journal%20of%20Peptide%20and%20Protein%20Research%2C%20Volume-46%281%20%281995%29%201-8.pdf
Muralidhara, B. K. and Prakash, V. (1995) Interaction of 3'-0-caffeoyal D-quinic acid with human serum albumin. International Journal of Peptide and Protein Research, 46 (1). pp. 1-8. |
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