共 81 条
Binding of small molecules at interface of protein-protein complex - A newer approach to rational drug design
被引:22
作者:
Gurung, A. B.
[1
]
Bhattacharjee, A.
[1
]
Ali, M. Ajmal
[2
]
Al-Hemaid, F.
[2
]
Lee, Joongku
[3
]
机构:
[1] North Eastern Hill Univ, Dept Biotechnol & Bioinformat, Shillong 793022, Meghalaya, India
[2] King Saud Univ, Dept Bot & Microbiol, Coll Sci, Riyadh 11451, Saudi Arabia
[3] Chungnam Natl Univ, Dept Environm & Forest Resources, 99 Daehak Ro, Daejeon 34134, South Korea
关键词:
Hot spots;
Protein interfaces;
Druggability;
Orthosteric inhibitor;
Allosteric inhibitor;
Interfacial binding inhibitor;
BIOMOLECULAR INTERACTION ANALYSIS;
SURFACE-PLASMON RESONANCE;
HOT-SPOTS;
FREE-ENERGY;
INHIBITORS;
DATABASE;
RECOGNITION;
DISCOVERY;
POTENT;
DIMERIZATION;
D O I:
10.1016/j.sjbs.2016.01.008
中图分类号:
Q [生物科学];
学科分类号:
07 ;
0710 ;
09 ;
摘要:
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. (c) 2016 The Authors. Production and hosting by Elsevier B. V. on behalf of King Saud University. This is an open access article under the CC BY-NC-NDlicense (http://creativecommons.org/licenses/by-nc-nd/4.0/).
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页码:379 / 388
页数:10
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