1Department of Bioinformatics, Guru Nanak College, Velachery, Chennai-600 042, India
2Department of Biochemistry, Mohd. Sathak College of Arts and Science, Chennai-119, India
3Department of Bioinformatics, SRM University, Chennai, India
*Corresponding Author E-mail: vanuradha_2003@yahoo.co.in
Online published on 6 May, 2013.
Infections caused by Candida species are the most prevalent fungal infections of humans and are a serious concern for patients with compromised immune systems. The role of sterol mutations in the resistance of Candida albicans to antifungal agents has not been thoroughly investigated. The approach described here exemplifies the efforts directed towards the discovery of drug targets which could effectively reduce the resistance towards various antifungal drugs. The analyses were performed using various Insilco methods. The protein sequence of lanosterol 14-alpha – demethylase was retrieved from NCBI. Mutations were induced and characterized for various physicochemical properties. Domain analysis shows that among all mutations, G464S and R467K may have vital role in Antifungal drug resistance mechanisms. It was concluded from the results of physicochemical and structural analysis that the change of a single amino acid disrupts the structure of domain that leads to antifungal resistance and also alters the native structure of the protein.
Lanosterol demethylase, Candida albicans, Drug resistance, Mutational analysis, Protein Modelling