First, I want to congratulate you on your dedication to accomplish this really interesting work!
I have done a review of this interesting work, and I have a couple of questions that you may help me to answer:
Do you know or have an idea about the factors that determine the affinity of the rilpivirine analogs when they bind to the NNRTIs protein?
Is the affinity of the rilpivirine analogs for the NNRTIs protein modified by the trifluoromethoxy groups and the pi-pi interaction of the benzene rings?
First, I want to congratulate you on your dedication to accomplish this really interesting work!
I have done a review of this interesting work, and I have a couple of questions that you may help me to answer:
Do you know or have an idea about the factors that determine the affinity of the rilpivirine analogs when they bind to the NNRTIs protein?
Is the affinity of the rilpivirine analogs for the NNRTIs protein modified by the trifluoromethoxy groups and the pi-pi interaction of the benzene rings?
Greetings! Thank you for taking the time to look at our presentation.
In regards to your first question, there are a multitude of factors that affect binding affinity in the allosteric NNRTI binding pocket, such as non-covalent protein-ligand interactions. We have found that the most effective binders engage a number of key amino acids in the binding pocket with strong non-covalent interactions. For example, the high binding affinity of analog 4G can be attributed to halogen-pi interactions, hydrophobic interactions, and hydrogen bond interactions. The interactions between residues in the protein also affect binding pocket shape; for example, electrostatic interactions between charged residues E138 and K101 form a salt bridge and when mutated, the shape of the binding pocket changes due to loss of interactions.
Yes, the binding affinity of the rilpivirine analogs are increased by the presence of a trifluoromethoxy group. The NNRTI binding pocket contains aromatic amino acids F227, W229, Y181, and Y188, which are crucial for forming pi-pi interactions with the benzene ring of rilpivirine and our analogs, and these interactions also contribute to modifications in binding affinity.
Hi Jeslyn and Charissa,
Fantastic work! Congratulations!
I was wondering if you have thought about the impact on the half-life of these compounds when you introduce the trifluoromethoxy group.
Best,
Hi Jeslyn and Charissa,
Fantastic work! Congratulations!
I was wondering if you have thought about the impact on the half-life of these compounds when you introduce the trifluoromethoxy groups.
Best,
First, I want to congratulate you on your dedication to accomplish this really interesting work!
I have done a review of this interesting work, and I have a couple of questions that you may help me to answer:
Do you know or have an idea about the factors that determine the affinity of the rilpivirine analogs when they bind to the NNRTIs protein?
Is the affinity of the rilpivirine analogs for the NNRTIs protein modified by the trifluoromethoxy groups and the pi-pi interaction of the benzene rings?
judge@sigmaxi.org
First, I want to congratulate you on your dedication to accomplish this really interesting work!
I have done a review of this interesting work, and I have a couple of questions that you may help me to answer:
Do you know or have an idea about the factors that determine the affinity of the rilpivirine analogs when they bind to the NNRTIs protein?
Is the affinity of the rilpivirine analogs for the NNRTIs protein modified by the trifluoromethoxy groups and the pi-pi interaction of the benzene rings?
judge@sigmaxi.org