Related Experiment Video
Updated: May 9, 2025
11:02
Genetic Encoding of a Non-Canonical Amino Acid for the Generation of Antibody-Drug Conjugates Through a Fast Bioorthogonal Reaction
Published on: September 14, 2018
7.7K
Unlocking ADAMTS-5: In Silico insights into TMJ proteomics and docking dynamics
Anjusha Divakar1, Nagachandran Kandasamy1, Remmiya Mary Varghese1
1Department of Orthodontics and Dentofacial Orthopaedics, Saveetha Dental College and Hospitals, Saveetha Institute of Medical and Technical Sciences, Saveetha University, Chennai, Tamil Nadu, India.
Journal of Orthodontic Science
|April 30, 2025
Summary
Researchers identified two promising compounds, ZINC1846088 and ZINC33606904, using molecular docking to target ADAMTS-5 protein for Temporomandibular joint (TMJ) disorder treatment.
Area of Science:
- Computational chemistry and drug discovery.
- Biochemistry and molecular modeling.
Background:
- Temporomandibular joint (TMJ) disorder involves pain and dysfunction in the jaw joint, with causes including injury, bruxism, arthritis, and stress.
- Computer-aided drug design (CADD) and molecular docking are crucial for understanding drug-molecule interactions and developing targeted therapies.
Purpose of the Study:
- To identify potential inhibitors for ADAMTS-5 protein implicated in TMJ disorder using molecular docking.
- To evaluate novel compounds against a selected ADAMTS-5 protein target.
Main Methods:
- Utilized molecular docking to screen 20 novel compounds against an optimized ADAMTS-5 protein target.
- Obtained compound structures from the Zinc15 database and protein structure from RCSB Protein Data Bank.
- Performed pharmacophore modeling to identify candidate molecules.
Main Results:
- Two compounds, ZINC1846088 and ZINC33606904, demonstrated the highest binding energy.
- These compounds exhibited superior binding properties compared to other screened molecules.
Conclusions:
- ZINC1846088 and ZINC33606904 show significant binding affinity to ADAMTS-5 protein.
- These molecules represent promising leads for developing targeted drug therapies for TMJ disorder.
Related Concept Videos
01:42The ADP/ATP Carrier Protein
3.1K
ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
3.1K
02:26tRNA Activation
18.7K
Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
18.7K
01:19Translocation of Proteins into the Mitochondria
3.0K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
3.0K
01:15Activation of Integrins
3.2K
Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
3.2K