Cystine-rich heterodimeric peptides or small proteins, such as insulin and relaxin are attractive targets for development of next-generation therapeutics owing to their pleiotropic physiological roles.1 The chemical synthesis of cystine-rich heterodimeric peptides has been an area of interest for many years.2,3 However, the crucial aspect for making these agents is that they need multiple solid phase synthesis of individual polypeptide chains, which makes the chemical synthesis of these large peptides (such as insulin-like peptides, peptide-peptide conjugates, etc.) a labour intensive and tedious process. We envisaged the use of chemically cleavable linker at the N-terminus of first polypeptide will allow the synthesis of second polypeptide chain on the same solid support.4 This general method of building two polypeptide chain on solid phase can be applied to any heterodimeric peptide conjugates. This novel bis-linker being compatible with various bio-conjugation and disulfide bond forming conditions is an efficient tool for solid phase peptide synthesis of modern peptide based therapeutics. The recent progress in the N-terminal cleavable linker strategy and its application in the synthesis of designer peptides, and peptide conjugates will be reported.
References:
1) Benítez (2014) Multifaceted Roles of Disulfide Bonds. Peptides as Therapeutics. Rev. 114: 901–926.
2) Belgi et. al (2011) The Chemical Synthesis of Insulin: From the Past to the Present. Immun. Endo. Met. Agents Med. Chem. 11:40-47.
3) Sohma et. al. (2009) Biomimetic Synthesis of Lispro Insulin via Chemically Synthesized Mini-proinsulin Prepared by Oxime Forming Ligation. J. Am. Chem. Soc. 131: 16313-16318.
4) Patil et. al. (2016) A One-Pot Chemically Cleavable Bis-Linker Tether Strategy for the Synthesis of Heterodimeric Peptides. Angew. Chem. Intl. Ed. 55:14552-14556.