Abstract:
Introduction:Compound D and DMPBD are compounds extracted from Plai or Zingiber cassumunar Roxb., which have antiasthmatic properties. Thai herbal pharmacopoeia have indicated that approximate 50% of Thai prescriptions for asthma contain Plai. However, the inhibition mechanisms of these compounds are not clearly known. Methods:In this study, molecular docking and molecular dynamics (MD) simulations have been used to simulate complex systems and analyze molecular interactions between these compounds and protein target, 5-lipoxygenase (5-LO) enzyme, which is an enzyme involved with asthma symptoms. Results:From our MD simulations, Compound D and DMPBD molecules bind at the same binding site of its natural substrate (arachidonic acid) on 5-LO enzyme, which is similar to the binding of commercial asthma drug (Zileuton). Molecular mechanics generalized born surface area binding energy calculations of the 5-LO complex with Compound D and DMPBD are -26.83 and -29.15 kcal/mol, respectively. Conclusions:This work indicated that Compound D and DMPBD are competitive inhibitors, which are able to bind at the same 5-LO substrate binding site. This reveals opportunities for using Compound D and DMPBD as novel antiasthmatic drugs.
journal_name
Cell Mol Bioengjournal_title
Cellular and molecular bioengineeringauthors
Jitapunkul K,Poachanukoon O,Hannongbua S,Toochinda P,Lawtrakul Ldoi
10.1007/s12195-017-0515-6subject
Has Abstractpub_date
2017-11-17 00:00:00pages
77-89issue
1eissn
1865-5025issn
1865-5033pii
515journal_volume
11pub_type
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