Letters in Drug Design & Discovery

Atta-ur-Rahman  , FRS
Honorary Life Fellow
Kings College
University of Cambridge
Email: lddd@benthamscience.org


The Inhibition of Acetylshikonin on Bacteria and its Trypsin-like Protease and Glycosidic Enzyme may be Essential to Conquer Periodontal Ecological Niche

Author(s): Ming-Yu Li, Laikuan Zhu, Guang-Yun Lai, Sisu Mo and Jun Wang

Affiliation: Shanghai Key Laboratory of Stomatology, Shanghai Research Institute of Stomatology, Ninth People’s Hospital, Medical College, Shanghai Jiao Tong University, 639 Zhizaoju Road, Shanghai 200011, P. R. China.

Graphical Abstract:


Background/Purposes: The objective of this study was to evaluate the inhibitory effects of acetylshikonin on bacteria in periodontal disease and the activities of trypsin-like protease and glycosidic enzyme of P. gingivalis in vitro.

Methods: The inhibition activity of acetylshikonin against bacteria was identified by microbial sensitivity tests of broth dilution method on 96-microwell plate. Trypsin-like protease and glycosidic enzyme activities were measured by a fluorescence spectrophotometer.

Results: The minimum inhibitory concentration of acetylshikonin on gram-negative were found to be 0.0625mg/ml, 0.125mg/ml, 0.125mg/ml, 0.25mg/ml, 0.25mg/ml and 0.5mg/ml, for S. intermedius, P. micros, P. acnes, L. acidophilus, A. viscosus and E. lentum respectively. Acetylshikonin showed extensive antibacterial activity against gram-negative bacteria, and it was more active against gram-positive bacteria. The acetylshikonin inhibited the activities of both trypsin-like protease and glycosidic enzyme by 45% and 95% with the final concentration of acetylshikonin from 0.0195 to 2.5 mg/ml.

Conclusion: The inhibition activity of acetylshikonin on bacteria and its enzyme of trypsin-like protease and glycosidic may be essential to conquer periodontal ecological niche for treating periodontal disease.

Keywords: Acetylshikonin, glycosidicological, in vitro, niche, trypsin-like protease.

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Article Details

Page: [1162 - 1166]
Pages: 5
DOI: 10.2174/1570180811666140704173134