SuperSweet—a resource on natural and artificial sweetening agents

A vast number of sweet tasting molecules are known, encompassing small compounds, carbohydrates, d-amino acids and large proteins. Carbohydrates play a particularly big role in human diet. The replacement of sugars in food with artificial sweeteners is common and is a general approach to prevent cavities, obesity and associated diseases such as diabetes and hyperlipidemia. Knowledge about the molecular basis of taste may reveal new strategies to overcome diet-induced diseases. In this context, the design of safe, low-calorie sweeteners is particularly important. Here, we provide a comprehensive collection of carbohydrates, artificial sweeteners and other sweet tasting agents like proteins and peptides. Additionally, structural information and properties such as number of calories, therapeutic annotations and a sweetness-index are stored in SuperSweet. Currently, the database consists of more than 8000 sweet molecules. Moreover, the database provides a modeled 3D structure of the sweet taste receptor and binding poses of the small sweet molecules. These binding poses provide hints for the design of new sweeteners. A user-friendly graphical interface allows similarity searching, visualization of docked sweeteners into the receptor etc. A sweetener classification tree and browsing features allow quick requests to be made to the database. The database is freely available at: http://bioinformatics.charite.de/sweet/.

[1]  V. Chatsudthipong,et al.  Stevioside and related compounds: therapeutic benefits beyond sweetness. , 2009, Pharmacology & therapeutics.

[2]  C. Hayes,et al.  The effect of non-cariogenic sweeteners on the prevention of dental caries: a review of the evidence. , 2001, Journal of dental education.

[3]  T. N. Bhat,et al.  The Protein Data Bank , 2000, Nucleic Acids Res..

[4]  P. Temussi,et al.  From small sweeteners to sweet proteins: anatomy of the binding sites of the human T1R2_T1R3 receptor. , 2005, Journal of medicinal chemistry.

[5]  Erik L. L. Sonnhammer,et al.  Predicting protein function from domain content , 2008, Bioinform..

[6]  Maria Kontoyianni,et al.  Evaluation of docking performance: comparative data on docking algorithms. , 2004, Journal of medicinal chemistry.

[7]  Yanli Wang,et al.  PubChem: a public information system for analyzing bioactivities of small molecules , 2009, Nucleic Acids Res..

[8]  P. Temussi The sweet taste receptor: a single receptor with multiple sites and modes of interaction. , 2007, Advances in food and nutrition research.

[9]  V. Diehl,et al.  Artificial sweeteners--do they bear a carcinogenic risk? , 2004, Annals of oncology : official journal of the European Society for Medical Oncology.

[10]  Didier Rognan,et al.  Comparative evaluation of eight docking tools for docking and virtual screening accuracy , 2004, Proteins.

[11]  Shin-Ichiro Nishimura,et al.  Glycoconjugate Data Bank:Structures—an annotated glycan structure database and N-glycan primary structure verification service , 2007, Nucleic Acids Res..

[12]  Christian Senger,et al.  Representation of target-bound drugs by computed conformers: implications for conformational libraries , 2006, BMC Bioinformatics.

[13]  S. Nakanishi,et al.  Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor , 2000, Nature.

[14]  Matthew P Campbell,et al.  GlycoExtractor: a web-based interface for high throughput processing of HPLC-glycan data. , 2010, Journal of proteome research.

[15]  Robert C. Edgar,et al.  MUSCLE: multiple sequence alignment with high accuracy and high throughput. , 2004, Nucleic acids research.

[16]  Martin Frank,et al.  GLYCOSCIENCES.de: an Internet portal to support glycomics and glycobiology research. , 2006, Glycobiology.

[17]  Pauline M. Rudd,et al.  GlycoBase and autoGU: tools for HPLC-based glycan analysis , 2008, Bioinform..

[18]  H. Schiöth,et al.  The Repertoire of G-Protein–Coupled Receptors in Fully Sequenced Genomes , 2005, Molecular Pharmacology.

[19]  Dariusz Plewczynski,et al.  Can we trust docking results? Evaluation of seven commonly used programs on PDBbind database , 2011, J. Comput. Chem..

[20]  Xiaodong Li,et al.  Different functional roles of T1R subunits in the heteromeric taste receptors. , 2004, Proceedings of the National Academy of Sciences of the United States of America.

[21]  P. Temussi,et al.  Why are sweet proteins sweet? Interaction of brazzein, monellin and thaumatin with the T1R2‐T1R3 receptor , 2002, FEBS letters.

[22]  R. Osman,et al.  Lactisole Interacts with the Transmembrane Domains of Human T1R3 to Inhibit Sweet Taste* , 2005, Journal of Biological Chemistry.

[23]  Roman Osman,et al.  Identification of the Cyclamate Interaction Site within the Transmembrane Domain of the Human Sweet Taste Receptor Subunit T1R3*[boxs] , 2005, Journal of Biological Chemistry.

[24]  P. Albersheim,et al.  Letter to the Glyco-Forum CarbBank , 1992 .

[25]  Andreas Bohne,et al.  SWEET-DB: an attempt to create annotated data collections for carbohydrates , 2002, Nucleic Acids Res..

[26]  Martin Frank,et al.  Glycome-DB.org: a portal for querying across the digital world of carbohydrate sequences. , 2009, Glycobiology.

[27]  Michelle Meadows,et al.  Advancing public health through partnerships. , 2006, FDA consumer.

[28]  Jan M.C. Geuns,et al.  Molecules of Interest Stevioside , 2003 .

[29]  B. Rost Twilight zone of protein sequence alignments. , 1999, Protein engineering.

[30]  R. M. HICKS,et al.  Co-carcinogenic Action of Saccharin in the Chemical Induction of Bladder Cancer , 1973, Nature.

[31]  R. Dwek,et al.  Glycobiology , 2018, Biochimie.

[32]  David Benton,et al.  Can artificial sweeteners help control body weight and prevent obesity? , 2005, Nutrition Research Reviews.

[33]  Hiren J. Joshi,et al.  GlycoSuiteDB: a curated relational database of glycoprotein glycan structures and their biological sources. 2003, update , 2003, Nucleic Acids Res..

[34]  Carolyn de la Peña Artificial sweetener as a historical window to culturally situated health , 2010, Annals of the New York Academy of Sciences.

[35]  Richard D. Taylor,et al.  Improved protein–ligand docking using GOLD , 2003, Proteins.

[36]  Midori Takasaki,et al.  Cancer preventive agents. Part 8: Chemopreventive effects of stevioside and related compounds. , 2009, Bioorganic & medicinal chemistry.

[37]  A. Drewnowski,et al.  Intense sweeteners and energy density of foods: implications for weight control , 1999, European Journal of Clinical Nutrition.

[38]  T. Blundell,et al.  Comparative protein modelling by satisfaction of spatial restraints. , 1993, Journal of molecular biology.

[39]  Kiyoko F. Aoki-Kinoshita,et al.  A global representation of the carbohydrate structures: a tool for the analysis of glycan. , 2005, Genome informatics. International Conference on Genome Informatics.

[40]  W M Edgar,et al.  Sugar substitutes, chewing gum and dental caries--a review , 1998, British Dental Journal.

[41]  Alessandro Pandini,et al.  Predicting the accuracy of protein–ligand docking on homology models , 2011, J. Comput. Chem..