Sentence examples for most potent interaction from inspiring English sources

Peptides VP1-6, VP1-8 and VP3-4 showed the most potent interaction, while peptides VP1-2 and VP2-2 interacted more weakly (Fig. 3A).

In agreement with the 3-drug experiment, TMP and GEN were identified to have the most potent interaction in the 5-drug and 6-durg experiments using both regression models.

The most potent interaction was observed with β-cardiac myosin with half-maximal activation (AC50) observed at 7.0 ± 1.5 µM EMD 57033 (Table 1).

Especially, WL-15 was one of the most potent inhibitors, blocking the interaction of MLL1 WDR5 with IC50 value of 26.4 nM in competitive binding assay and inhibiting the catalytic activity of MLL1 complex with IC50 value of 5.4 μM.

We showed that nelfinavir was the most potent inhibitor of the interaction process between L. amazonensis and macrophage cells, showing a clear dose-dependent inhibition profile, where the inhibition increased from 86 to 93% (in relation to control) as nelfinavir concentration rose from 50 to 100 µM.

It is also one of the most potent platelet activators through interaction of protease-activated receptors (PARs) on the platelet surface [ 10].

For this we used sequences derived from the translesion DNA polymerase UmuC and the DNA replication initiation factor Hda that out of a panel of 15 peptide sequences were the most potent inhibitors of the interaction between the polymerase and clamp (Wijffels et al., 2004) (see Materials and methods for more details).

The bias towards the lower G-content in the unstructured sequences was not surprising, because guanine is the most potent in base-paring interactions: it forms a triple hydrogen bond with cytosine and a wobble pair with uracil.

Fig. 4 The post docking interaction map of most potent antifungal compound 4o (magenta) exhibiting multiple types of interactions involving hydrophobic, π π and electrostatic interactions (red lines) with the significant residues of antifungal target protein N-myristoyl transferase enzyme (light blue) from C. albicans.

The most potent inhibitor has several favorable interactions with the binding site and induces the P-loop to fold inward, creating a significant hydrophobic enclosure for itself.

The interaction between the most potent compound of the series and the c-myc G-quadruplex was examined in depth using UV Vis titration, molecular modeling and CD spectroscopy.