Receptor pharmacology fundamentals
Receptor pharmacology fundamentals: 5 articles from Peptides Facts. Evidence-led reference on research peptides.
Orthosteric or Allosteric: Where a Peptide Ligand Binds and Why It Changes the Pharmacology
A ligand occupying the site the natural hormone uses competes with it. A ligand binding somewhere else modulates it. The two produce different ceilings, different dependence on the endogenous signal, and different failure modes.
Biased Agonism: G-Protein Versus β-Arrestin Signalling at Peptide Receptors
Two agonists can occupy the same receptor and produce different mixtures of downstream signal. That observation dismantled the idea of a receptor as an on-off switch, and it is the reason two compounds with identical targets can behave differently over time.
Concentration–Response: EC50, Emax, and Why Potency and Efficacy Are Not the Same Number
Two compounds can be compared on where their curve sits and on how high it reaches. Those are independent properties, they answer different questions, and treating one as a proxy for the other is the most common misreading in this literature.
Desensitisation, Internalisation and Downregulation: Three Things That Get Called "Tolerance"
A falling response to a repeated stimulus has at least four possible causes operating on different timescales. They are routinely reported under one word, and the word chosen usually reveals nothing about which process was measured.
Selectivity: How a Peptide Chooses Its Receptor, and What Happens When It Does Not
Selectivity is a ratio between numbers measured at two receptors, and it survives only within the range of concentrations where that ratio holds. Most claims of selectivity in this field are missing both the comparison and the range.