title: Traceless reductive ligation at a tryptophan site: a facile access to β-hydroxytryptophan appended peptides.
abstract: An efficient methodology for cysteine-free ligation at a tryptophan (Trp) site is described. A chemically active scaffold, β-hydroxy-α-azidotryptophan, has been synthesized and explored towards the synthesis of a series of β-hydroxytryptophan appended native peptides in good yields via one-pot reductive traceless ligation of β-O-peptidyl-α-azidotryptophan involving an O → N peptidyl transfer strategy. Pre-organized conformational analysis and reaction energy pathway based theoretical studies further supported the experimental findings on the chemical structure stability of ligated products.
authors.affiliation: Department of Chemistry, Birla Institute of Technology and Science, Pilani 333031, Rajasthan, India. Kbajaj26@gmail.com.
authors.forename: Kiran
authors.initials: K
authors.lastname: Bajaj
authors.affiliation: Department of Chemistry, Birla Institute of Technology and Science, Pilani 333031, Rajasthan, India. Kbajaj26@gmail.com.
authors.forename: Rajeev
authors.initials: R
authors.lastname: Sakhuja
authors.affiliation: Institute of Chemistry, University of Tartu, Tartu 50411, Estonia.
authors.forename: Girinath G
authors.initials: GG
authors.lastname: Pillai
mesh_terms: D006916:5-Hydroxytryptophan / Q000737:chemistry*; D008958:Models, Molecular; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry*
chemical_list: D010455:Peptides; D006916:5-Hydroxytryptophan