Abstract

Binding between bovine serum albumin (BSA) and a plumeran indole alkaloid (PIA) isolated from the stem bark of Aspidosperma cylindrocarpon (Apocynaceae) was studied by spectroscopic techniques (UV-Vis absorption, circular dichroism, steady state and time-resolved fluorescence), combined with molecular docking. Steady state and time resolved fluorescence data revealed that PIA can quench the BSA fluorescence via a static mechanism: energy transfer from BSA to PIA occurs with high probability. The binding is strong (Kb ca. 105-106 L mol-1), spontaneous (ΔG° ca. -35.7 kJ mol-1 at 310 K) and entropy-driven (ΔS° = 0.146 kJ mol-1 K-1). There is just one main binding site (n ca. 1) for the BSA:PIA interaction and the α-helix content of the albumin does not suffer significant perturbation upon PIA binding. Molecular docking results suggest site I as the main binding site to PIA, which is able to interact with the Trp-212, Arg-217, Val-342 and Pro-446 residues.

Highlights

  • The Apocynaceae family consists of 424 genera, divided into 17 tribes that are subdivided into five subfamilies: Rauwolfioideae, Apocynoideae, Asclepioideae, Periplocoideae and Secamonioideae

  • The interaction of plumeran indole alkaloid (PIA) with bovine serum albumin (BSA) was monitored by studying the fluorescence quenching of BSA with increasing PIA concentrations

  • A small red shift is observed upon increasing PIA concentration, which suggests an increase in the hydrophobicity of the microenvironment around the tryptophan residue to which PIA is associated.[20]

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Summary

Introduction

The Apocynaceae family consists of 424 genera, divided into 17 tribes that are subdivided into five subfamilies: Rauwolfioideae, Apocynoideae, Asclepioideae, Periplocoideae and Secamonioideae. About 400 species of Apocynaceae have been identified and grouped into 41 genera in Brazil, 78% of which are found only in the Amazonia region,[1] among them, Aspidosperma cylindrocarpon from the Polyneura series (popularly known in Brazil as “peroba-osso” or “peroba-rosa”) It has a high content of indole alkaloids and has been extensively studied in phytochemistry and pharmacology.[2] Many indole alkaloids with distinct biological activities are described in the literature; among. SA is a multifunctional protein with ligand binding capacity, making it a transporter molecule for a diverse range of metabolites, drugs, nutrients, metals and other molecules. Due to their ligand binding properties, albumins have wide clinical, pharmaceutical, Studies of the Interaction between BSA and a Plumeran Indole Alkaloid

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