title: Butelase-Mediated Ligation as an Efficient Bioconjugation Method for the Synthesis of Peptide Dendrimers.
abstract: Herein we report a novel enzymatic bioconjugation method to prepare peptide dendrimers. Under the catalysis of a newly discovered peptide ligase, butelase 1, peptide dendrimers of di-, tetra-, and octabranches were successfully synthesized using thiodepsipeptides as acyl donors for ligation with lysyl dendrimeric scaffolds. The efficient assembly of the highly clustered dendrimeric structure highlighted the versatility of butelase 1. We also showed that our synthetic antibacterial peptide dendrimers containing an RLYR motif are highly potent and broadly active against antibiotic-resistant strains.
authors.affiliation: School of Biological Sciences, Nanyang Technological University , 60 Nanyang Drive, Singapore 637551.
authors.forename: Yuan
authors.initials: Y
authors.lastname: Cao
authors.affiliation: School of Biological Sciences, Nanyang Technological University , 60 Nanyang Drive, Singapore 637551.
authors.forename: Giang K T
authors.initials: GK
authors.lastname: Nguyen
authors.affiliation: School of Biological Sciences, Nanyang Technological University , 60 Nanyang Drive, Singapore 637551.
authors.forename: Samuel
authors.initials: S
authors.lastname: Chuah
authors.affiliation: School of Biological Sciences, Nanyang Technological University , 60 Nanyang Drive, Singapore 637551.
authors.forename: James P
authors.initials: JP
authors.lastname: Tam
authors.affiliation: School of Biological Sciences, Nanyang Technological University , 60 Nanyang Drive, Singapore 637551.
authors.forename: Chuan-Fa
authors.initials: CF
authors.lastname: Liu
mesh_terms: D000595:Amino Acid Sequence; D060326:Chemistry Techniques, Synthetic; D050091:Dendrimers / Q000737:chemistry*; D008025:Ligases / Q000378:metabolism*; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry* / Q000378:metabolism
chemical_list: D050091:Dendrimers; D010455:Peptides; D008025:Ligases