Search results
Results from the WOW.Com Content Network
Once a cyclic peptide is identified with a biological activity of interest, it may also be possible to identify the target of the peptide (a gene that encodes a protein with which it interacts) by functional complementation, facilitating a better understanding of its mechanism of action.
Crystal structure of an extracellular segment of integrin alphaVbeta3 complexed with a cyclic peptide containing the arginyl-glycyl-aspartic acid (RGD) sequence. RGD is shown in maroon. CEND-1, also known as iRGD, is a cyclic peptide that homes to tumors via binding to integrin alpha V receptors. [22]
During the course of the docking process, the ligand and the protein adjust their conformation to achieve an overall "best-fit" and this kind of conformational adjustment resulting in the overall binding is referred to as "induced-fit". [5] Molecular docking research focuses on computationally simulating the molecular recognition process.
Coarse-grained models are often implemented in the case of protein-peptide docking, as they frequently involve large-scale conformation transitions of the protein receptor. [7] [8] AutoDock is one of the computational tools frequently used to model the interactions between proteins and ligands during the drug discovery process. Although the ...
With advances in the generation of very large synthetic cyclic peptide libraries and in vitro affinity-based selection methods, [2] scientists have begun to harness the potential of this molecular modality as a template for novel ligands in drug development and other applications. However, while approaches in de novo discovery of synthetic high ...
α-Amanitin Bacitracin Ciclosporin. Cyclic peptides are polypeptide chains which contain a circular sequence of bonds. [1] This can be through a connection between the amino and carboxyl ends of the peptide, for example in cyclosporin; a connection between the amino end and a side chain, for example in bacitracin; the carboxyl end and a side chain, for example in colistin; or two side chains ...
Macromolecular docking is the computational modelling of the quaternary structure of complexes formed by two or more interacting biological macromolecules. Protein–protein complexes are the most commonly attempted targets of such modelling, followed by protein–nucleic acid complexes.
After determining the peptide sequence of the lectin protein favin, they noticed its similarity to a known protein – concanavalin A – except that the ends were circularly permuted. Later work confirmed the circular permutation between the pair [ 2 ] and showed that concanavalin A is permuted post-translationally [ 3 ] through cleavage and ...