title: α-glucosidase and glycation inhibitory effects of costus speciosus leaves.
abstract: BACKGROUND
  Hyperglycaemia is a salient feature of poorly controlled diabetes mellitus. Rate of protein glycation is increased with hyperglycaemia leading to long term complications of diabetes. One approach of controlling blood glucose in diabetes targets at reducing the postprandial spikes of blood glucose. The objectives of this study were to assess the in vitro inhibitory effects of Costus speciosus (COS) leaves on α-amylase and α-glucosidase activities, fructosamine formation, protein glycation and glycation-induced protein cross-linking.
  
  
  METHODS
  Methanol extracts of COS leaves were used. Inhibitory effects on enzyme activities were measured using porcine pancreatic α-amylase and α-glucosidase from Saccharomyces cerevisiae in the presence of COS extract. Percentage inhibition of the enzymes and the IC50 values were determined. In vitro protein glycation inhibitory effect of COS leaves on early and late glycation products were measured using bovine serum albumin or chicken egg lysozyme with fructose. Nitroblue tetrazolium was used to assess the relative concentration of fructosamine and polyacrylamide gel electrophoresis was used to assess the degree of glycation and protein cross-linking in the reaction mixtures.
  
  
  RESULTS
  α-Glucosidase inhibitory activity was detected in COS leaves with a IC50 of 67.5 μg/ml which was significantly lower than the IC50 value of Acarbose (p < 0.01). Amylase inhibitory effects occurred at a comparatively higher concentration of extract with a IC50 of 5.88 mg/ml which was significantly higher than the IC50 value of Acarbose (p < 0.01). COS (250 μg/ml) demonstrated inhibitory effects on fructosamine formation and glycation induced protein cross-linking which were in par with 1 mg/ml aminoguanidine were detected.
  
  
  CONCLUSIONS
  Methanol extracts of COS leaves demonstrated in vitro inhibitory activities on α-glucosidase, fructosamine formation, glycation and glycation induced protein cross-linking. These findings provide scientific evidence to support the use of COS leaves for hypoglycemic effects with an added advantage in slowing down protein glycation.
authors.affiliation: Department of Biochemistry, Faculty of Medicine, University of Peradeniya, Peradeniya, Sri Lanka. kumudup@pdn.ac.lk.
authors.forename: Handunge Kumudu Irani
authors.initials: HK
authors.lastname: Perera
authors.affiliation: Department of Biochemistry, Faculty of Medicine, University of Peradeniya, Peradeniya, Sri Lanka. wkvpremadasa@gmail.com.|Postgraduate Institute of Science, University of Peradeniya, Peradeniya, Sri Lanka. wkvpremadasa@gmail.com.
authors.forename: Walgama Kankanamlage Vindhya Kalpani
authors.initials: WK
authors.lastname: Premadasa
authors.affiliation: Department of Biochemistry, Faculty of Medicine, University of Peradeniya, Peradeniya, Sri Lanka. jpoongunran@gmail.com.|Postgraduate Institute of Science, University of Peradeniya, Peradeniya, Sri Lanka. jpoongunran@gmail.com.
authors.forename: Jeyakumaran
authors.initials: J
authors.lastname: Poongunran
mesh_terms: D029770:Costus / Q000737:chemistry*; D019270:Fructosamine / Q000096:biosynthesis; D017127:Glycation End Products, Advanced / Q000378:metabolism; D065089:Glycoside Hydrolase Inhibitors / Q000494:pharmacology*; D006031:Glycosylation / Q000187:drug effects; D018515:Plant Leaves; D000516:alpha-Amylases / Q000037:antagonists & inhibitors*; D000520:alpha-Glucosidases / Q000378:metabolism
chemical_list: D017127:Glycation End Products, Advanced; D065089:Glycoside Hydrolase Inhibitors; D019270:Fructosamine; D000516:alpha-Amylases; D000520:alpha-Glucosidases