email   Email Us: phone   Call Us: +1 (914) 407-6109   57 West 57th Street, 3rd floor, New York - NY 10019, USA

Lupine Publishers Group

Lupine Publishers

  Submit Manuscript

ISSN: 2637-4579

Open Access Journal of Biomedical Engineering and Biosciences

Research Article(ISSN: 2637-4579)

Binding Model of Antidiabetic Constituents from Capsosiphon fulvescens with Human Aldose Reductase

Volume 1 - Issue 2

Ogunwa Tomisin Happy1,2*

  • Author Information Open or Close
    • 1Centre for BioComputing and Drug Development, Adekunle Ajasin University, Nigeria
    • 2Department of Biochemistry, Adekunle Ajasin University, Nigeria

    *Corresponding author: Ogunwa Tomisin Happy, Centre for BioComputing and Drug Development, Adekunle Ajasin University, Akungba-Akoko, Ondo State, Nigeria

Received: February 13, 2018;   Published: February 21, 2018

DOI: 10.32474/OAJBEB.2018.01.000110

Full Text PDF

To view the Full Article   Peer-reviewed Article PDF


The use of seaweeds as functional foods and drugs is well known. Capsosiphon fulvescens (C. fulvescens) is a green sea algafor which beneficial health impacts have been reported even in diabetes. In the present study, three C. fulvescens constituents (chalinasterol, capsofulvesin A and capsofulvesin B) were evaluated for their molecular binding signature and interaction patterns against human aldose reductase as an antidiabetic target. The enzyme has been robustly implicated in the development of secondary complications of diabetes. The results generated here with the aid of in silico tools revealed a favourable binding affinity for the seawed constituents on the active site of aldose reductase. However, detailed observation shows no interference with the NADP binding pocket. The binding configuration of capsofulvesin A and capsofulvesin B were comparable to fidarestatas the compounds inserted one of their elongated aliphatic long chains with double bondsinto the binding pocket. Nonetheless, subtle differences were sighted with the binding format of the aliphatic chain of capsofulvesin B resulting froma possiblehydrophobic hinderanceor influence within the binding pocket. Only one of the aliphatic chainsof capsofulvesin A enjoyed hydrophobic interaction with residues Val47, Trp219 and Phe122 compared to the capsofulvesin B having hydrophobic interaction with Phe122 at the second chain while the other aliphatic chain formed hydrophobicbond with Trp20, Val47, Trp219 and Leu300. Meanwhile, the galactoseunit of the two compounds displayed similar binding orientation and interaction with amino acid residues Ser22 and Trp20 at the active site. Chalinasterol, on the other hand, established hydrogen bond with the imidazole ring of His110 and indole ring of Trp111 respectively. The current study represents the first attempt to model the interaction of these ligands with aldose reductase and theunique bindingpatterns might explain the mechanism and potency of C. fulvescens in themanagement of diabetes and its complications.

Keywords: Capsosiphon fulvescens; Aldose reductase; Molecular interaction; Capsofulvesin A; Capsofulvesin B; Chalinasterol

Abbrevations: NADP: Nicotinamide Adenosine Diphosphate; 3D: Three Dimensional

Abstract| Introduction| Materials and Methods| Results and Discussion| Conclusion| References|