Unknown

Dataset Information

0

Binding of small molecules at interface of protein-protein complex - A newer approach to rational drug design.


ABSTRACT: 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 both in silico as 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.

SUBMITTER: Gurung AB 

PROVIDER: S-EPMC5272936 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Binding of small molecules at interface of protein-protein complex - A newer approach to rational drug design.

Gurung A B AB   Bhattacharjee A A   Ajmal Ali M M   Al-Hemaid F F   Lee Joongku J  

Saudi journal of biological sciences 20160107 2


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 both <i>in silico</i> as 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 druggabilit  ...[more]

Similar Datasets

2015-11-02 | E-MTAB-2948 | biostudies-arrayexpress
| S-EPMC149879 | biostudies-literature
| S-EPMC9474704 | biostudies-literature
| S-EPMC10510469 | biostudies-literature
| S-EPMC1978269 | biostudies-other
| S-EPMC9261181 | biostudies-literature
| S-EPMC3169948 | biostudies-literature
| S-EPMC5584760 | biostudies-literature
| S-EPMC6272512 | biostudies-literature
| S-EPMC5039900 | biostudies-literature