Zorzi, AlessandroLinciano, SaraAngelini, Alessandro2019-08-012019-08-012019-08-012019-07-0110.1039/c9md00018fhttps://infoscience.epfl.ch/handle/20.500.14299/159481WOS:000475806000002Peptides and small protein scaffolds are gaining increasing interest as therapeutics. Similarly to full-length antibodies, they can bind a target with a high binding affinity and specificity while remaining small enough to diffuse into tissues. However, despite their numerous advantages, small biotherapeutics often suffer from a relatively short circulating half-life, thus requiring frequent applications that ultimately restrict their ease of use and user compliance. To overcome this limitation, a large variety of half-life extension strategies have been developed in the last decades. Linkage to ligands that non-covalently bind to albumin, the most abundant serum protein with a circulating half-life of similar to 19 days in humans, represents one of the most successful approaches for the generation of long-lasting biotherapeutics with improved pharmacokinetic properties and superior efficacy in the clinic.Biochemistry & Molecular BiologyChemistry, MedicinalPharmacology & Pharmacyhuman serum-albuminsingle-chain diabodypharmacokinetic propertiescrystallographic analysisdomain antibodiesdisplay selectionaffibody moleculedependent bindingpeptidefusiontext::journal::journal article::review article