Background: Caesalpinia bonducella L. is a medicinal plant belonging to the family Caesalpiniaceae. It is a prickly shrub widely distributed all over the world especially in Indian tropical regions such as Kerala, Andaman and Nicobar Islands and Sri Lanka. There are claims that its leaves or seeds/ seed kernel possess antipyretic, antidiuretic, antibacterial, antiviral, antiestrogenic and antidiabetic activities. Due to the above properties several preparations of the plant were used in folk medicine. Materials and Methods: The aqueous extract of Caesalpinia bonducella nut containing the seed and the shell, has been evaluated for qualitative analysis of secondary metabolites (tannis, flavonoids, alkaloids, saponins, coumarins, quinone and phenols), in-vitro anti-inflammatory, anti-diabetic assay, antioxidant, antimitotic and antimicrobial activity. The studies were carried out using HRBC membrane stabilization, inhibition of alpha amalyse enzyme, DPPH method, green gram growth inhibition, agar diffusion method respectively. Results: Our results indicate the presence of Alkaloids, Flavanoids and Saponins. We report in our study the antidiabetic, anti-inflammatory, anti-oxidant, anti-microbial and antimitotic activity of Caesalpinia bonducella. ABSTRACT SUMMARY• The study reported the presence of various Alkaloids, Flavonoids and Saponins in the seed/shell of Caesalpinia bonducella L. Due to the presence of these bioactive compounds, the seed and the shell extracts showed antidiabetic, anti-inflammatory, anti-oxidant, anti-microbial and anti-mitotic activity. C bonducella can thus be used as an adjunct therapy for inflammation and diabetes.The use of C bonducella seed extract for the treatment of cancer requires further research.

Aluminium and zinc are known to be the major triggering agents for aggregation of amyloid peptides leading to plaque formation in Alzheimer's disease. While zinc binding to histidine in Aβ (amyloid β) fragments has been implicated as responsible for aggregation, not much information is available on the interaction of aluminium with histidine. In the NMR study of the N-terminal Aβ fragments, DAEFRHDSGYEV (Aβ12) and DAEFRHDSGYEVHHQK (Aβ16) presented here, the interactions of the fragments with aluminium have been investigated. Significant chemical shifts were observed for few residues near the C-terminus when aluminium chloride was titrated with Aβ12 and Aβ16 peptides. Surprisingly, it is nonhistidine residues which seem to be involved in aluminium binding. Based on NMR constrained structure obtained by molecular modelling, aluminium-binding pockets in Aβ12 were around charged residues such as Asp, Glu. The results are discussed in terms of native structure propagation, and the relevance of histidine residues in the sequences for metal-binding interactions. We expect that the study of such short amyloid peptide fragments will not only provide clues for plaque formation in aggregated conditions but also facilitate design of potential drugs for these targets.

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Alzheimer's disease (AD) is characterized by neurofibrillary tangles (NFTs), formed as a consequence of hyperphosphorylation of tau. The extent of phosphorylation of tau is regulated by protein phosphatases (PPs) like PP1, PP2A/Bα, PP2B and PP5. Interestingly, PP2A/Bα, is a major brain tau phosphatase which account for 70% of the dephosphorylation events in brain and, its activity is known to decrease by half under AD conditions. The down regulation of PP2A leads to hyperphosphorylation of Tau in the brains of AD patients. Hence, the process of reversal of tau phosphorylation needs to be achieved by the activation of PP2A, through specific molecules, as this could pave way towards development of novel therapeutics for AD. The key objective

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