Development of novel renin inhibitors and interaction of
Transcript of Development of novel renin inhibitors and interaction of
FAKULTY OF SCIENCE AND TECHNOLOGY DEPARTMENT OF CHEMISTRY
Development of novel renin inhibitors and interaction of antimicrobial and cytotoxic peptides with plasma proteins A drug discovery study
Annfrid Sivertsen
A dissertation for the degree of Philosophiae Doctor April 2013
FAKULTY OF SCIENCE AND TECHNOLOGY DEPARTMENT OF CHEMISTRY
Development of novel renin inhibitors and interaction of antimicrobial and cytotoxic peptides with plasma proteins A drug discovery study
Annfrid Sivertsen
A dissertation for the degree of Philosophiae Doctor April 2013
Figure 14. The figure shows the comparison of the phenotype F1*S and A of AGP, in a) for phenotype
F1*S and in b) for phenotype A respectively. Both the pattern of polar residues and shape of the
binding pocket are altered, with the binding site of phenotype A lacking sub-pocket III due to changes
in side chain conformations of sub-site III residues. The binding site is located in the middle of the
figures, with the binding site section viewed to the right for closer inspection. The electrostatic surface
potential is shown for both phenotypes. Reprint from Nishi et al. 2011 [149], with permission from the
American Society for Biochemistry and Molecular Biology.