Binding of small molecules at interface of protein-protein complex - A newer approach to rational drug design.
Protein-protein interaction is a vital process which drives many important physiological processes in the cell and has also been implicated in several diseases. Though the protein-protein interaction network is quite complex but understanding its interacting partners using bothin silicoas well as molecular biology techniques can provide better insights for targeting such interactions. Targeting protein-protein interaction with small molecules is a challenging task because of druggability issues. Nevertheless, several studies on the kinetics as well as thermodynamic properties of protein-protein interactions have immensely contributed toward better understanding of the affinity of these complexes. But, more recent studies on hot spots and interface residues have opened up new avenues in the drug discovery process. This approach has been used in the design of hot spot based modulators targeting protein-protein interaction with the objective of normalizing such interactions.
Department of Biotechnology and Bioinformatics, North Eastern Hill University, Shillong 793022, Meghalaya, India.
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Gurung
Department of Biotechnology and Bioinformatics, North Eastern Hill University, Shillong 793022, Meghalaya, India.
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Bhattacharjee
Department of Botany and Microbiology, College of Science, King Saud University, Riyadh 11451, Saudi Arabia.
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Ajmal Ali
Department of Botany and Microbiology, College of Science, King Saud University, Riyadh 11451, Saudi Arabia.
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Al-Hemaid
Department of Environment and Forest Resources, Chungnam National University, 99 Daehak-ro, Yuseong-gu, Daejeon 34134, Republic of Korea.
Joongku
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Lee
Allosteric inhibitor; Druggability; Hot spots; Interfacial binding inhibitor; Orthosteric inhibitor; Protein interfaces