Lunminlal Kipgen, Sugandha Saxena, Kamal K Aggarwal
University School of Biotechnology, Guru Gobind Singh Indraprastha University, Dwarka-16C, New Delhi, India.


The functional information of peptidase inhibitors reside within a few peptides at the reactive site. Reactive sites of serine, cysteine and carboxypeptidase inhibitors were structurally compared. Protein molecules inhibiting the same class of peptidases were found to have structurally conserved reactive sites. Carboxypeptidase-A inhibitors (CPI) insert their C- or N-terminals into the enzyme active sites.

Peptidase-protein inhibitor docking was performed. Statistically significant correlations were observed between inhibitory constants (Ki) and docking energy scores. Bound docking of Cysteine peptidases (Papain family) with conjugate inhibitors gave a correlation coefficient of 0.943 and P value of 0.0167. Increase in Ki value was correlated with rise in binding energy.Read more…

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