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Chelerythrine–lysozyme interaction: spectroscopic studies, thermodynamics and molecular modeling exploration

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Title Chelerythrine–lysozyme interaction: spectroscopic studies, thermodynamics and molecular modeling exploration
 
Creator Jash, Chandrima
Basu, Pritha
Payghan, Pavan V.
Ghoshal, Nanda
Kumar, Gopinatha Suresh
 
Subject Chemistry
 
Description The binding of the iminium and alkanolamine forms of chelerythrine to lysozyme (Lyz) was investigated by spectroscopy and docking studies. The thermodynamics of the binding was studied by calorimetry. Spectroscopic evidence suggested that Trp-62 and Trp-63 in the b-domain of the protein are closer to the binding site; moreover, the binding site was at a distance of 2.27 and 2.00 nm from the iminium and alkanolamine forms, respectively, according to the Forster theory of non-radiation energy transfer. The
equilibrium binding constants for the iminium and alkanolamine forms at 298 K were evaluated to be 1.29 � 105 and 7.79 � 105 M�1, respectively. The binding resulted in an alteration of the secondary structure of the protein with a distinct reduction of the helical organization. The binding of iminium was endothermic, involving electrostatic and hydrophobic interactions, while that of alkanolamine form was exothermic and dominated by hydrogen bonding interactions. Docking studies provided the atomistic
details pertaining to the binding of both forms of chelerythrine and supported the higher binding in
favour of the alkanolamine over the iminium. Furthermore, molecular dynamics study provided accurate insights regarding the binding of both chelerythrine forms in accordance with the experimental results obtained. Chelerythrine binding pocket involves the catalytic region and aggregation prone K-peptide region, which are sandwiched between one another. Overall, these results suggest that both the forms of the alkaloid bind to the protein but the neutral form has higher affinity than the cationic form.
 
Date 2015
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/2248/1/PHYSICAL_CHEMISTRY_CHEMICAL_PHYSICS__V._17___(_25)_16630%2D16645;2015[82].pdf
Jash, Chandrima and Basu, Pritha and Payghan, Pavan V. and Ghoshal, Nanda and Kumar, Gopinatha Suresh (2015) Chelerythrine–lysozyme interaction: spectroscopic studies, thermodynamics and molecular modeling exploration. Physical Chemistry Chemical Physics, 17 (25). pp. 16630-16645.
 
Relation http://dx.doi.org/10.1039/c5cp00424a
http://www.eprints.iicb.res.in/2248/