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Molecular Docking of Bacosides with Tryptophan Hydroxylase:A Model to Understand the Bacosides Mechanism

Natural Products and Bioprospecting 2014年第4期4卷 251-255页

作者： David Mary Rajathei jayakumar preethi Hemant K.Singh Koilmani Emmanuvel Rajan Department of Bioinformtics Bharathidasan UniversityTiruchirappalli 620024India Department of Animal Science School of Life SciencesBharathidasan UniversityTiruchirappalli 620024India Laboratories of CNS Disorder Learning&MemoryDivision of PharmacologyCentral Drug Research InstituteLucknow 226031India

Tryptophan hydroxylase(TPH)catalyses L-tryptophan into 5-hydroxy-L-tryptophan,which is the first and ratelimiting step of serotonin(5-HT)***,we found that TPH2 up-regulated in the hippocampus of postnatal rats after the oral treatment of Bacopa monniera leaf extract containing the active compound ***,the knowledge about the interactions between bacosides with TPH is *** this study,we take advantage of in silico approach to understand the interaction of bacoside-TPH complex using three different docking algorithms such as HexDock,PatchDock and *** these three algorithms showed that bacoside A and A3 well fit into the cavity consists of active ***,our analysis revealed that major active compounds bacoside A3 and A interact with different residues of TPH through hydrogen ***,Tyr235,Thr265 and Glu317 are the key residues among them,but none of them are either at tryptophan or BH4 binding ***,its note worthy to mention that Tyr 235 is a catalytic sensitive residue,Thr265 is present in the flexible loop region and Glu317 is known to interacts with *** with these residues may critically regulate TPH function and thus serotonin *** study suggested that the interaction of bacosides(A3/A)with TPH might up-regulate its activity to elevate the biosynthesis of 5-HT,thereby enhances learning and memory formation.

关键词： Serotonin Tryptophan hydroxylase Bacosides Docking

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