Abstract:
:Molecular dynamics simulations, binding free energy calculations, principle component analysis (PCA), and residue interaction network analysis were employed in order to investigate the molecular mechanism of M184I single mutation which played pivotal role in making the HIV-1 reverse transcriptase (RT) totally resistant to lamivudine. Results showed that single mutations at residue 184 of RT caused (1) distortion of the orientation of lamivudine in the active site due to the steric conflict between the oxathiolane ring of lamivudine and the side chain of beta-branched amino acids Ile at position 184 which, in turn, perturbs inhibitor binding, (2) decrease in the binding affinity by (~8 kcal/mol) when compared to the wild-type, (3) variation in the overall enzyme motion as evident from the PCA for both systems, and (4) distortion of the hydrogen bonding network and atomic interactions with the inhibitor. The comprehensive analysis presented in this report can provide useful information for understanding the drug resistance mechanism against lamivudine. The results can also provide some potential clues for further design of novel inhibitors that are less susceptible to drug resistance.
journal_name
Cell Biochem Biophysjournal_title
Cell biochemistry and biophysicsauthors
Moonsamy S,Bhakat S,Walker RC,Soliman MEdoi
10.1007/s12013-015-0709-2subject
Has Abstractpub_date
2016-03-01 00:00:00pages
35-48issue
1eissn
1085-9195issn
1559-0283pii
10.1007/s12013-015-0709-2journal_volume
74pub_type
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