Francis X. Farrell

TL;DR: Random phage display peptide libraries and affinity selective methods were used to isolate small peptides that bind to and activate the receptor for the cytokine erythropoietin (EPO) and these peptides appear to be identical to those induced by the natural ligand.

TL;DR: Comparison of the biological properties of agonist and antagonist EMPs with EPO suggests that the extracellular domain orientation is tightly coupled to the cytoplasmic signaling events and provides valuable new insights into the design of synthetic ligands for EPOR and other cytokine receptors.

TL;DR: A chemically defined, dimeric form of an erythropoietin mimetic peptide (EMP) that displays 100-fold increased affinity for the EPOR and correspondingly elevated potency in cell-based assays and in mice is synthesized.

TL;DR: A 13 amino acid peptide was identified which possesses mimetic properties and contains a minimal agonist epitope, and the ability of this peptide to effectively serve as a mimetic capable of the induction of EPO-responsive cell proliferation appears to reside within a single residue.

TL;DR: The potency of previously isolated peptides that are modest agonists of the EPO receptor was dramatically increased by PEG-induced dimerization, and the conversion of an inactive peptide into an agonist further supports the idea thatDimerization can mediate receptor activation.