Drug Targets Lecture Dr David Davies 2024

what is the strongest intermolecular bond?

electrostatic/ioninc bond

where does an ionic bond typically occur?

between a protonated amine and a deprotonated acid

what is the pka of amine?

10

what is the pka of acids

4

what amino acid is always protonated at physiological pka 7?

arginine and lysisne

what amino acid is always can act as both an acid and base?

histadine as it can be both protonated and non protonated at physiological ph

what hetero atoms can form hydrogen bonds?

nitrogen, oxgen, flourine( weaK)

what are some examples of strong hydrogen bond acceptors and why?

COO- and PO4- as they are negatively charged so attract the hydrogen bond donor much more strongly

how does a hydrogen bond form?

directional orbital overlap (180 degrees)

what are hydrophobic interactions/van der waals?

weak, non specific surface dependent interactions

how does entropy loss work against binding?

when drugs bind to their target they lose entropy as they become less disordered. the greater the entropy loss the less activity the drug will show. this is important in drugs that can rotate.

what is the difference between enzyme/substrate and receptors/agonist intercation?

the substrate is chemically changes by the enzyme giving the product, the agonist is not chemically changes and is released from the receptor. binding in both cases is non covalent.

what is residence time?

the period of time the agonist is bound to the receptor. this also determines how good the binding is

what are allosteric anatgonists?

drugs that bind to the allosteric site and cause a confirmational change to the orthostatic site, preventing binding of the drug

what amino acids are deprotonated at physiological pH?

aspartate and glutamate

what amino acids are protonated at physiological pH?

lysine and arginine