Amino acid similarity, between statin binding site of hmg coa reductase and taste perception-related proteins: A possible mechanism for statin-induced taste disorders

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Objective: Statins are widely prescribed worldwide and used by millions of people to decrease blood cholesterol level. Taste disorders are among many documented side effects of statins and reported in less than 2% of the patients who use a statin. The molecular mechanism of statin-induced taste disorders is not known. In this study, a bioinformatics approach was used for the elucidation of this mechanism. Material and Method: In order to gain insight into the mechanism of statin-induced taste disorders, we searched human protein database by using Basic Local Alignment Search Tool (BLAST) and 3-hydroxy-3- methylglutarylcoenzyme A reductase QiMGCR) as query.Results: Our search revealed two proteins: Polycystic kidney disease 1 like 1 (PKD1L1) and transcription factor AP-2 beta (TFAP2B) both of which are involved in taste perception. Our results suggest a possible partial interaction between statins and PKD1L1 and TFAP2B. Conclusion: Further studies such as molecular docking and identification of statin binding proteins by affinity column chromatography using statins as substrate can clarify the contribution of such an interaction to the mechanisms of statin induced taste disorders.

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dc.contributor.authorVural, Mutlu
dc.contributor.authorOlgun, Abdullah
dc.date.accessioned2026-10-18T20:30:46.588240617Z
dc.date.available2026-10-18T20:30:46.588240617Z
dc.date.issued2012
dc.description.abstractObjective: Statins are widely prescribed worldwide and used by millions of people to decrease blood cholesterol level. Taste disorders are among many documented side effects of statins and reported in less than 2% of the patients who use a statin. The molecular mechanism of statin-induced taste disorders is not known. In this study, a bioinformatics approach was used for the elucidation of this mechanism. Material and Method: In order to gain insight into the mechanism of statin-induced taste disorders, we searched human protein database by using Basic Local Alignment Search Tool (BLAST) and 3-hydroxy-3- methylglutarylcoenzyme A reductase QiMGCR) as query.Results: Our search revealed two proteins: Polycystic kidney disease 1 like 1 (PKD1L1) and transcription factor AP-2 beta (TFAP2B) both of which are involved in taste perception. Our results suggest a possible partial interaction between statins and PKD1L1 and TFAP2B. Conclusion: Further studies such as molecular docking and identification of statin binding proteins by affinity column chromatography using statins as substrate can clarify the contribution of such an interaction to the mechanisms of statin induced taste disorders.
dc.identifier.endpage107
dc.identifier.issn1305-2381
dc.identifier.issue3
dc.identifier.scopus2-s2.0-84872953314
dc.identifier.startpage105
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/ebyu/15930
dc.identifier.volume8
dc.language.isoen
dc.relation.ispartofNobel Medicus
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectPolycystic kidney disease 1 like 1 protein (PKD1L1)
dc.subjectStatins
dc.subjectTaste disorder
dc.subjectTranscription factor AP-2 betaprotein
dc.subjectatorvastatin
dc.subjecthydroxymethylglutaryl coenzyme A reductase
dc.subjecthydroxymethylglutaryl coenzyme A reductase inhibitor
dc.subjectpolycystic kidney disease 1 like 1 protein
dc.subjecttranscription factor AP 2
dc.subjecttranscription factor AP 2 beta
dc.subjectunclassified drug
dc.subjectamino acid sequence
dc.subjectarticle
dc.subjectbioinformatics
dc.subjectcolumn chromatography
dc.subjectdrug binding site
dc.subjectdrug mechanism
dc.subjectmolecular docking
dc.subjectnonhuman
dc.subjectprescription
dc.subjectprotein analysis
dc.subjectprotein domain
dc.subjecttaste
dc.titleAmino acid similarity, between statin binding site of hmg coa reductase and taste perception-related proteins: A possible mechanism for statin-induced taste disorders
dc.typeArticle
dspace.entity.typePublication
rdl.citation.scopus0
rdl.source.indexSCOPUS