Abstract: Many synthetic peptides have been developed for diagnosis and therapy of human cancers\nbased on their ability to target specific receptors on cancer cell surface or to penetrate the cell\nmembrane. Chemical modifications of amino acid chains have significantly improved the biological\nactivity, the stability and efficacy of peptide analogues currently employed as anticancer drugs or as\nmolecular imaging tracers. The stability of somatostatin, integrins and bombesin analogues in the\nhuman body have been significantly increased by cyclization and/or insertion of non-natural amino\nacids in the peptide sequences. Moreover, the overall pharmacokinetic properties of such analogues\nand others (including cholecystokinin, vasoactive intestinal peptide and neurotensin analogues)\nhave been improved by PEGylation and glycosylation. Furthermore, conjugation of those peptide\nanalogues to new linkers and bifunctional chelators (such as AAZTA, TETA, TRAP, NOPO etc.),\nproduced radiolabeled moieties with increased half life and higher binding affinity to the cognate\nreceptors. This review describes the most important and recent chemical modifications introduced in\nthe amino acid sequences as well as linkers and new bifunctional chelators which have significantly\nimproved the specificity and sensitivity of peptides used in oncologic diagnosis and therapy.
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