Electrostatic recognition between enzyme and inhibitor: interaction between papain and leupeptin.
Electrostatic forces are involved in a wide variety of molecular interactions that are of biological interest, including, among others, DNA-Protein interactions, protein folding, and the interactions between enzymes and their substrates and inhibitors. In this work, the interaction between papain and an inhibitor, leupeptin, is analyzed from the point of view of their electrostatic interaction. The computations enable one to suggest that negatively charged amino acids located in the region of the active site are responsible for creating an environment that enables efficient binding of the inhibitor. This binding occurs despite the fact that the net global charge of both molecules is positive; an explanation for this apparent contradiction is proposed.
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Departamento de Física, Universidad Nacional del Sur, Bahía Blanca, Argentina.
Vallejo
D F
DF
Grigera
J R
JR
D001665:Binding Sites / Q000502:physiology; D003198:Computer Simulation; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry*; D007976:Leupeptins / Q000737:chemistry*; D046911:Macromolecular Substances; D008956:Models, Chemical; D008958:Models, Molecular; D010206:Papain / Q000037:antagonists & inhibitors / Q000737:chemistry*; D011485:Protein Binding / Q000502:physiology; D055672:Static Electricity
D015853:Cysteine Proteinase Inhibitors; D007976:Leupeptins; D046911:Macromolecular Substances; D010206:Papain; C032854:leupeptin