[null, null, {"document_url": "http://cipsm.de/publications/research-area-e/rational-design-of-an-anticalin-type-sugar-binding-protein-using-a-genetically-encoded-boronate-side-chain/", "unformatted_src": "/site/assets/files/8043/skerra_acs-sb17_550.jpeg", "src": "https://cipsm.de/site/assets/files/8043/skerra_acs-sb17_550.jpeg", "formatted_filename": "skerra acs sb"}, {"document_url": "http://cipsm.de/publications/research-area-e/rational-design-of-an-anticalin-type-sugar-binding-protein-using-a-genetically-encoded-boronate-side-chain/", "unformatted_src": "/site/templates/images/cipsm_movie_155_grau.jpg", "src": "https://cipsm.de/site/templates/images/cipsm_movie_155_grau.jpg", "formatted_filename": "cipsm movie grau", "alt_text": "CIPSM Movie"}, {"document_url": "http://cipsm.de/publications/research-area-e/rational-design-of-an-anticalin-type-sugar-binding-protein-using-a-genetically-encoded-boronate-side-chain/", "unformatted_src": "/site/templates/images/LMUexcellent.png", "src": "https://cipsm.de/site/templates/images/LMUexcellent.png", "formatted_filename": "LMUexcellent", "alt_text": "LMUexcellent"}, {"document_url": "http://cipsm.de/publications/research-area-e/rational-design-of-an-anticalin-type-sugar-binding-protein-using-a-genetically-encoded-boronate-side-chain/", "unformatted_src": "/site/templates/images/TU_Muenchen.png", "src": "https://cipsm.de/site/templates/images/TU_Muenchen.png", "formatted_filename": "TU Muenchen", "alt_text": "TU M\u00fcnchen"}, {"document_url": "http://cipsm.de/publications/research-area-e/rational-design-of-an-anticalin-type-sugar-binding-protein-using-a-genetically-encoded-boronate-side-chain/", "unformatted_src": "/site/templates/images/MPG.png", "src": "https://cipsm.de/site/templates/images/MPG.png", "formatted_filename": "MPG", "alt_text": "MPG"}, {"document_url": "http://cipsm.de/publications/research-area-e/rational-design-of-an-anticalin-type-sugar-binding-protein-using-a-genetically-encoded-boronate-side-chain/", "unformatted_src": "/site/templates/images/Helmholz_Muenchen.png", "src": "https://cipsm.de/site/templates/images/Helmholz_Muenchen.png", "formatted_filename": "Helmholz Muenchen", "alt_text": "Helmholtz M\u00fcnchen"}, {"document_url": "http://cipsm.de/publications/research-area-e/rational-design-of-an-anticalin-type-sugar-binding-protein-using-a-genetically-encoded-boronate-side-chain/", "unformatted_src": "/site/templates/images/MPI_of_Neurobiology.png", "src": "https://cipsm.de/site/templates/images/MPI_of_Neurobiology.png", "formatted_filename": "MPI of Neurobiology", "alt_text": "MPI of Neurobiology"}, {"document_url": "http://cipsm.de/publications/research-area-e/rational-design-of-an-anticalin-type-sugar-binding-protein-using-a-genetically-encoded-boronate-side-chain/", "unformatted_src": "/site/templates/images/MPI_of_Biochemistry.png", "src": "https://cipsm.de/site/templates/images/MPI_of_Biochemistry.png", "formatted_filename": "MPI of Biochemistry", "alt_text": "MPI of Biochemistry"}, null]
Rational Design of an Anticalin-Type Sugar-Binding Protein Using a Genetically Encoded Boronate Side Chain


Selvakumar Edwardraja, Andreas Eichinger, Ina Theobald, Carina Andrea Sommer, Andreas J. Reichert, Arne Skerra

ACS Synth. Biol., 2017, 6 (12), pp 2241–2247, DOI: 10.1021/acssynbio.7b00199
ACS Synth. Biol., online article

The molecular recognition of carbohydrates plays a fundamental role in many biological processes. However, the development of carbohydrate-binding reagents for biomedical research and use poses a challenge due to the generally poor affinity of proteins toward sugars in aqueous solution. Here, we describe the effective molecular recognition of pyranose monosaccharides (in particular, galactose and mannose) by a rationally designed protein receptor based on the human lipocalin scaffold (Anticalin). Complexation relies on reversible covalent cis-diol boronate diester formation with a genetically encoded l-boronophenylalanine (Bpa) residue which was incorporated as a non-natural amino acid at a sterically permissive position in the ligand pocket of the Anticalin, as confirmed by X-ray crystallography. Compared with the metal-ion and/or avidity-dependent oligovalent lectins that prevail in nature, our approach offers a novel and promising route to generate tight sugar-binding reagents both as research reagents and for biomedical applications.