Binding studies of valganciclovir to human serum albumin by multispectroscopic techniques (Record no. 8453)

MARC details
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fixed length control field a
003 - CONTROL NUMBER IDENTIFIER
control field OSt
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20190315092752.0
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 190307b xxu||||| |||| 00| 0 eng d
040 ## - CATALOGING SOURCE
Original cataloging agency AIKTC-KRRC
Transcribing agency AIKTC-KRRC
100 ## - MAIN ENTRY--PERSONAL NAME
9 (RLIN) 7889
Author Somaji, Lade
245 ## - TITLE STATEMENT
Title Binding studies of valganciclovir to human serum albumin by multispectroscopic techniques
250 ## - EDITION STATEMENT
Volume, Issue number Vol. 10(10), July-August
260 ## - PUBLICATION, DISTRIBUTION, ETC.
Place of publication, distribution, etc. M. P.
Name of publisher, distributor, etc. Innovare Academic Sciences Pvt Ltd
Year 2018
300 ## - PHYSICAL DESCRIPTION
Pagination 87-92
520 ## - SUMMARY, ETC.
Summary, etc. Objective:The aim of the present study was to investigate the mode and mechanism of interactions involved towards binding of valganciclovir (VGC) with Human Serum Albumin (HSA) by spectroscopic and molecular modeling studies which can be extrapolated for the ten folds increase of bioavailability over its prodrug galanciclovir. Methods: Herein we employed fluorescence spectroscopy for evaluating the binding constant value, site of interaction and changes in the microenvironment of HSA fluorophores. Circular dichroism (CD) and UV-Visible spectroscopy is used for conformational changes of HSA in the event of binding of valaganciclovir. These experimental studies were further corroborated with molecular modeling studies. Results: Considerable quenching of fluorescence intensities of fluorophores in the presence of VGC showed that VGC interacts with HSA strongly with a binding constant of 4.11x104 M-1Conclusion:The weaker dominant electrostatic interactions with minor contributions of hydrophobic interactions of VGC with HSA at site IB (catalytic domain) might be the probable reason for the relative increase of hydrolysis of VGC to galanciclovir. And moderate binding constant value with HSA implies that HSA can be able to transport VGC under physiological conditions. with a free energy change of-6.26 Kcal/mol. Synchronous fluorescence and CD studies show that the microenvironment and confirmation of HSA are slightly altered in the presence of VGC. Though site marker experiments does not give any clue for identification of site, molecular docking studies showed that VGC binds to site IB of HSA
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
9 (RLIN) 4639
Topical term or geographic name entry element PHARMACEUTICS
700 ## - ADDED ENTRY--PERSONAL NAME
9 (RLIN) 7890
Co-Author Rapolu, Ravi
773 0# - HOST ITEM ENTRY
Place, publisher, and date of publication Bhopal Innovare Academic Sciences Pvt Ltd
Title International journal of pharmacy and pharmaceutical science
International Standard Serial Number 0975 – 1491
856 ## - ELECTRONIC LOCATION AND ACCESS
URL https://innovareacademics.in/journals/index.php/ijpps/article/view/28090/15895
Link text Click here
942 ## - ADDED ENTRY ELEMENTS (KOHA)
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Koha item type Articles Abstract Database
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    Dewey Decimal Classification     School of Pharmacy School of Pharmacy Archieval Section 30/03/2019   2018423 19/06/2019 30/03/2019 Articles Abstract Database
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