Studies on Anti-Glycating effect of three varieties of finger millet (Eleusine coracona)

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Studies on anti-glycating effects of three varieties of

finger millet (Eleusine coracona)

G. Balaji

Anna University, Chennai, Tamil Nadu

Guided by

G. Bhanuprakash Reddy

ICMR-National Institute of Nutrition

Abstract

Diabetes and its associated pathologies has been a major speculation among growing

population in this world. Globally, an estimated 422 million adults were living with diabetes

in 2014, compared to 108 million in 1980. The global prevalence of diabetes has nearly

doubled since 1980, rising from 4.7 to 8.5% in the adult population. The prevalence of

diabetes is increasing as it would reach 300 million people worldwide in 2025 (WHO report

2016). Protein glycation due to Maillard reaction which sparks the formation of advanced

glycation end products is one of the major cause for the diabetic associated pathological

complications (Chi-Hao Wu et al., 2011). Inhibition of formation of AGE’s ameliorate

complications of diabetics such as neuropathy, nephropathy, retinopathy, cardio myopathy

etc (Singh et al.). Traditionally various whole cereal diet and also herbal supplements has

been long followed to prevent such diabetic complications. These Nutraceuticals and

functional foods have gained much importance in present world due to its potential

therapeutic values as it has propitious effect in alleviating diabetes. Finger millet one of the

minor cereal variety grown almost all parts of the country shows pacifying response in

allaying diabetic associated complications. This finger millet encompasses wide range

dietary fibres, carbohydrates with low glycaemic index and higher sustaining power, high

phytochemicals such as polyphenols, flavonoids, antioxidants etc. Recent studies of finger

millet on animal model manifests propitious effect of polyphenols in type 2 diabetes

(Shobana et al., 2010). In this study three different varieties of finger millet such as CO9,

CO14, GPU28 were chosen for investigation. Invitro AGE’s were synthesized with Bovine

serum albumin (BSA) and Methyl Glyoxal. In vitro analytical methods such as AGE and

tryptophan fluorescence, western blot, protein carbonyls, metal chelating activity, DPPH

assay, AR inhibitory assay (Saraswat et al., 2018) were employed. This study evidenced

salubrious effect of these three-millet’s polyphenolic extracts to be type 1 and type 2

inhibitors of AGE. We propose use of these nutraceuticals can benefit diabetics in

preventing associated health complications.

Abbreviations

AGE

Advanced Glycation Endproducts

APS

Ammonium Per Sulphate

BSA

Bovine Serum Albumin

CEL

Carboxy ethyl Lysine

CML

Carboxy Methyl Lysine

Deoxyglucosones

DNPH

2,4-Dinitro,Phenyl Hydrazine

DPPH

2,2-Diphenyl-picryl-Hydrazyl

EDTA

Ethylene Diamine Tetra Acetic Acid

FFI

2-(2-furoyl)-4(5)-(2-furanyl)-1-himidozole

GAE

Gallic Acid Equivalent

GOLD

Glyoxal Lysine Dimer

HCl

Hydrochlorc Acid

HRE

Heat Reflux Extract

MOLD

Methyl Glyoxal Lysine Dimer

PBS

Phosphate Buffer Saline

PBST

Phosphate Buffer Saline with Tween-20

Quercetin Equivalents

SDS- PAGE

Sodium Dodecyl Sulphate- Poly Acrylamide Gel

SMP

Skimmed Milk Powder

TCA

Trichloro Acetic Acid

TEMED

TetramethylethyleneDimer

UAE

Ultrasonic Assisted Extract

1. Introduction

Proteins are complex biomolecules in an organism which is a pivot of all physiochemical

processes. This word was first coined by Jons Jacob Berzelius from Greek word proteius

meaning holding first place. Proteins are the building blocks of our human system. Amino

acids are the fundamental backbone of proteins. There were about 20 amino acids which joins

in various configurations to form protein. Proteins are organ specific, therefore function of

protein is attributed to the structure and functions of amino acids in that protein chain. (Felix

Haurowitz, Daniel E. Koshland et al., Principles of Biochemistry, Leninger).

Protein functions as antibody that bind to specific foreign particles such as virus, bacteria and

provide us immunological barriers. Proteins act as enzymes which carries out thousands of

reactions that takes place in cells. They also assist in the formation of new molecules by

reading the genetic information stored in DNA for example phenyl alanine hydroxylase.

Proteins are sometimes messengers which aids in transmission of signals to co-ordinate

biological process between different cells, tissues and organs. These proteins also form the

structural basis of cells such as collagen.

Any alteration in structure of proteins will results in loss of function and formation of complex

products which leads to various forms of illness.

1.1. Basic structure of proteins

1.1.1. Primary Structure

The sequence of amino acids joined together by peptide bonds that make up a protein or

polypeptide chain is known as primary structure (Fig. 1). Peptide bonds are created by

enzyme catalysed condensation reactions and broken down by enzyme catalysed hydrolysis

reactions.

Fig. 1. Primary structure.

Fig. 2. (a) Beta pleated structure and (b) Alpha helix.