Topological, hydrophobicity, and other descriptors on alpha-glucosidase inhibition: a QSAR study on xanthone derivatives

• Type: Article in International Scientific Journal
• Date: 2011

Authors

Hari Narayana H N Moorthy (Author) Other; Maria J Ramos (Author) FCUP; Pedro A Fernandes (Author) FCUP

Journal

Title: Journal of Enzyme Inhibition and Medicinal Chemistry

Vol. 26 No. 1

Pages: 755-766

ISSN: 1475-6366

Publisher: Taylor & Francis

Indexing

ISI Web of Knowledge - 17 Citations

Scopus - 19 Citations

Scientific classification

FOS: Medical and Health sciences > Basic medicine

Other information

Authenticus ID: P-002-JC8

DOI: 10.3109/14756366.2011.549089

Abstract (EN): Quantitative structure activity relationship analysis was performed on a series of xanthone derivatives to establish the structural features required for alpha-glucosidase inhibitory activity. The computational and statistical analysis was performed with V life MDS (Molecular Design Suite) and Statistica software. The selected models show significant predictive power, stability, and reliability in terms of cross-validated correlation coefficient (Q(cv)(2) > 0.74 and Q(test)(2) > 0.5) and other validation parameters. The results show that the SaaaC count, MMFF_6 and dipole moment are mainly contributed for the activity along with the hydrophobicity descriptors. It describes that heteroatoms (oxygen atom connected with carbon atom) in the molecules are favourable for alpha-glucosidase inhibitory activity. The E-state count descriptor suggests that when carbon atoms connected with three aromatic bonds and hydrogen or other atoms are favourable for the activity. The SAHA and SAMH descriptors show that the hydrophilic area in the molecule is important for the activity while high hydrophilicity is unfavourable for the activity. This study concluded that hydrophilic, polar and/or electron negative groups, which are responsible for hydrogen bonding and interaction with the enzyme for favourable activity.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 12