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Issue Information
Publication year - 2018
Publication title -
peptide science
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.533
H-Index - 7
ISSN - 2475-8817
DOI - 10.1002/pep2.24039
Subject(s) - proteases , limiting , antibody , receptor , citation , peptide , protease , computer science , chemistry , computational biology , medicine , immunology , biology , biochemistry , enzyme , world wide web , engineering , mechanical engineering
Free peptides have little or no resistance to cleavage by serum/tissue proteases, leading to poor stability and thus limiting their use as therapeutics. Protease recognition can be avoided by conjugation to a fragment crystallizable (Fc) domain of immunoglobulin G (IgG), generating a peptibody that exhibits higher circulation time than the stand‐alone peptide(s). The mechanism of action of peptibodies also mimics therapeutic antibodies ‐ they can act directly on cell membranes, killing the cells, or with membrane/soluble receptors, activating/disabling cellular pathways. Neves et al . discuss the design and production of peptibodies, and highlight a number currently in preclinical and clinical development. (doi: 10.1002/bip.23095 )