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Systematic Biophysical Insights into the Interaction of Anti MERS-CoV Drug Ribavirin with Major Transport Protein in Human Serum: In-Vitro Studies and Implications in Diabetes and Uremia

Identifieur interne : 000574 ( Pmc/Corpus ); précédent : 000573; suivant : 000575

Systematic Biophysical Insights into the Interaction of Anti MERS-CoV Drug Ribavirin with Major Transport Protein in Human Serum: In-Vitro Studies and Implications in Diabetes and Uremia

Auteurs : Fahad Almutairi ; Mohammad Rehan Ajmal

Source :

RBID : PMC:7111155
Url:
DOI: 10.1016/j.bpj.2018.11.2593
PubMed: NONE
PubMed Central: 7111155

Links to Exploration step

PMC:7111155

Le document en format XML

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<title xml:lang="en">Systematic Biophysical Insights into the Interaction of Anti MERS-CoV Drug Ribavirin with Major Transport Protein in Human Serum: In-Vitro Studies and Implications in Diabetes and Uremia</title>
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<name sortKey="Almutairi, Fahad" sort="Almutairi, Fahad" uniqKey="Almutairi F" first="Fahad" last="Almutairi">Fahad Almutairi</name>
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<name sortKey="Rehan Ajmal, Mohammad" sort="Rehan Ajmal, Mohammad" uniqKey="Rehan Ajmal M" first="Mohammad" last="Rehan Ajmal">Mohammad Rehan Ajmal</name>
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<idno type="doi">10.1016/j.bpj.2018.11.2593</idno>
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<title xml:lang="en" level="a" type="main">Systematic Biophysical Insights into the Interaction of Anti MERS-CoV Drug Ribavirin with Major Transport Protein in Human Serum: In-Vitro Studies and Implications in Diabetes and Uremia</title>
<author>
<name sortKey="Almutairi, Fahad" sort="Almutairi, Fahad" uniqKey="Almutairi F" first="Fahad" last="Almutairi">Fahad Almutairi</name>
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<author>
<name sortKey="Rehan Ajmal, Mohammad" sort="Rehan Ajmal, Mohammad" uniqKey="Rehan Ajmal M" first="Mohammad" last="Rehan Ajmal">Mohammad Rehan Ajmal</name>
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<series>
<title level="j">Biophysical Journal</title>
<idno type="ISSN">0006-3495</idno>
<idno type="eISSN">1542-0086</idno>
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<date when="2019">2019</date>
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<journal-id journal-id-type="nlm-ta">Biophys J</journal-id>
<journal-id journal-id-type="iso-abbrev">Biophys. J</journal-id>
<journal-title-group>
<journal-title>Biophysical Journal</journal-title>
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<issn pub-type="ppub">0006-3495</issn>
<issn pub-type="epub">1542-0086</issn>
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<publisher-name>The Biophysical Society</publisher-name>
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<article-id pub-id-type="publisher-id">S0006-3495(18)33858-X</article-id>
<article-id pub-id-type="doi">10.1016/j.bpj.2018.11.2593</article-id>
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<subject>Article</subject>
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<title-group>
<article-title>Systematic Biophysical Insights into the Interaction of Anti MERS-CoV Drug Ribavirin with Major Transport Protein in Human Serum: In-Vitro Studies and Implications in Diabetes and Uremia</article-title>
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<contrib-group>
<contrib contrib-type="author" id="au1">
<name>
<surname>Almutairi</surname>
<given-names>Fahad</given-names>
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<contrib contrib-type="author" id="au2">
<name>
<surname>Rehan Ajmal</surname>
<given-names>Mohammad</given-names>
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<aff id="aff1">Biochemistry, University of Tabuk, Tabuk, Saudi Arabia</aff>
<pub-date pub-type="pmc-release">
<day>15</day>
<month>2</month>
<year>2019</year>
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<pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub">
<day>15</day>
<month>2</month>
<year>2019</year>
</pub-date>
<pub-date pub-type="epub">
<day>15</day>
<month>2</month>
<year>2019</year>
</pub-date>
<volume>116</volume>
<issue>3</issue>
<fpage>480a</fpage>
<lpage>480a</lpage>
<permissions>
<copyright-year>2018</copyright-year>
</permissions>
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<notes>
<p id="misc0010">2378-Pos</p>
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<body>
<p id="p0010">The effect of glycosylation in the interaction of antiviral drug ribavirin is studied in detail with major transport protein in blood, human serum albumin (HSA) under in vitro disease mimetic conditions. Ribavirin is an antiviral drug used in treatment of Middle East Respiratory Syndrome Coronavirus (MERS-CoV) infection in Tabuk region, kingdom of Saudi Arabia. In present study interaction mechanism for binding of ribavirin with HSA has been elucidated. We explored the binding interaction under physiological environment for alterations in their binding characteristics in co-morbid disease environments namely uremia and diabetes. Binding affinity for drug was found to decrease with glycosylation also there are conformational changes pertaining to binding of drug to target protein. To evaluate the drug binding defects we employed combination of biophysical and bioinformatics techniques. Fluorescence and UV-visible spectroscopy has been used to elucidate the parameters of the drug complexation in presence of urea and glucose. Binding of ribavirin to human serum albumin has been found to decrease both in uremia and diabetic mimetic conditions. Molecular topology of protein has also been studied by dynamic light scattering under different conditions. Ligand binding is an important phenomenon; it essentially controls drug pharmacokinetics. Treatment outcome in MERS-CoV infection have been strongly correlated to diabetes and chronic kidney disease. This study is an attempt to examine binding refashioning under these conditions and will help to understand the changes in drug behavior, this will help in dosage design; appropriate for achieving optimum therapeutic treatment outcome.</p>
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