{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Seebeck FP"],"funding":["NIGMS NIH HHS"],"pagination":["7150-1"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2572134"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["128(22)"],"pubmed_abstract":["Dehydroalanine is a nonproteinogenic amino acid, but it is a component of a wide variety of natural products with therapeutic activities. Indeed, this alpha,beta-unsaturated residue is a highly versatile building block due to its rigidifying effect on peptide backbones and its electrophilicity which allows site-specific thiol ligations of peptides with small molecules or proteins. To harness such versatility in genetically encoded, combinatorial peptide libraries, we report a simple and robust method for the ribosomal synthesis of dehydroalanine-containing peptides. Selenalysine, a selenium-containing lysine analogue, was recruited as a masked dehydroalanine equivalent. This residue is efficiently incorporated by a reconstituted Escherichia coli translation system at high fidelity and effi"],"journal":["Journal of the American Chemical Society"],"pubmed_title":["Ribosomal synthesis of dehydroalanine-containing peptides."],"pmcid":["PMC2572134"],"funding_grant_id":["F32 GM074505-02","F32 GM074505","GM 074505-02"],"pubmed_authors":["Seebeck FP","Szostak JW"],"additional_accession":[]},"is_claimable":false,"name":"Ribosomal synthesis of dehydroalanine-containing peptides.","description":"Dehydroalanine is a nonproteinogenic amino acid, but it is a component of a wide variety of natural products with therapeutic activities. Indeed, this alpha,beta-unsaturated residue is a highly versatile building block due to its rigidifying effect on peptide backbones and its electrophilicity which allows site-specific thiol ligations of peptides with small molecules or proteins. To harness such versatility in genetically encoded, combinatorial peptide libraries, we report a simple and robust method for the ribosomal synthesis of dehydroalanine-containing peptides. Selenalysine, a selenium-containing lysine analogue, was recruited as a masked dehydroalanine equivalent. This residue is efficiently incorporated by a reconstituted Escherichia coli translation system at high fidelity and effi","dates":{"release":"2006-01-01T00:00:00Z","publication":"2006 Jun","modification":"2025-04-22T06:46:49.667Z","creation":"2019-03-27T00:19:01Z"},"accession":"S-EPMC2572134","cross_references":{"pubmed":["16734454"],"doi":["10.1021/ja060966w"]}}