The rodlike virus M13 phage is nontoxic to humans. Its tip can be engineered to recognize a specific target and at the same time its sidewall can be engineered to electrostatically assemble drug‐loaded liposomes (see picture). The phage–liposome complex forms a drug carrier that can be internalized in breast cancer cells and used in photodynamic therapy.

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G-protein coupled receptors (GPCRs) are ubiquitous membrane proteins allowing intracellular response to extracellular factors that range from photons of light to small molecules to proteins. Despite extensive exploitation of GRCRs as therapeutic targets, biophysical characterization of GPCR-ligand interactions remains challenging. In this minireview, we focus on techniques which have been successfully employed for structural and biophysical characterization of peptide ligands binding to their cognate GPCRs. The techniques reviewed include solution-state nuclear magnetic resonance (NMR) spectroscopy; solid-state NMR; X-ray diffraction; fluorescence spectroscopy and single molecule fluorescence methods; flow cytometry; surface plasmon resonance; isothermal titration calorimetry; and, atomic force microscopy. The goal herein is to provide a cohesive starting point to allow selection of techniques appropriate to the elucidation of a given GPCR-peptide interaction.