| Affiliation: | 1. Departament de Química Analítica i Química Orgànica, Facultat de Química, Universitat Rovira i Virgili, C/ Marcel⋅lí Domingo 1, 43007 Tarragona, Spain
Department of Chemistry, Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford, OX1 3TA UK;2. Departament de Química Analítica i Química Orgànica, Facultat de Química, Universitat Rovira i Virgili, C/ Marcel⋅lí Domingo 1, 43007 Tarragona, Spain;3. Department of Chemistry, Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford, OX1 3TA UK |
| Abstract: | Methods that site-selectively attach multivalent carbohydrate moieties to proteins can be used to generate homogeneous glycodendriproteins as synthetic functional mimics of glycoproteins. Here, we study aspects of the scope and limitations of some common bioconjugation techniques that can give access to well-defined glycodendriproteins. A diverse reactive platform was designed via use of thiol-Michael-type additions, thiol-ene reactions, and Cu(I)-mediated azide-alkyne cycloadditions from recombinant proteins containing the non-canonical amino acids dehydroalanine, homoallylglycine, homopropargylglycine, and azidohomoalanine. |
