Additional file 6 of Genome sequencing and molecular networking analysis of the wild fungus Anthostomella pinea reveal its ability to produce a diverse range of secondary metabolites

Additional file 6: List of hits from GNPS MS/MS library search of A. pinea extracts

Additional file 4 of Genome sequencing and molecular networking analysis of the wild fungus Anthostomella pinea reveal its ability to produce a diverse range of secondary metabolites

Additional file 4: Molecular network of A. pinea F5 extracts and annotation by Sirius (Cytoscape session file)

CCDC 1912181: Experimental Crystal Structure Determination

Related Article: Qian Wang, Angelina Osipyan, Markella Konstantinidou, Roberto Butera, Kumchok C. Mgimpatsang, Svitlana V. Shishkina, Alexander Dömling|2019|J.Org.Chem.|84|12148|doi:10.1021/acs.joc.9b0125

CCDC 1912182: Experimental Crystal Structure Determination

Related Article: Qian Wang, Angelina Osipyan, Markella Konstantinidou, Roberto Butera, Kumchok C. Mgimpatsang, Svitlana V. Shishkina, Alexander Dömling|2019|J.Org.Chem.|84|12148|doi:10.1021/acs.joc.9b0125

Liposome functionalization with copper-free "click chemistry"

The modification of liposomal surfaces is of interest for many different applications and a variety of chemistries are available that makes this possible. A major disadvantage of commonly used coupling chemistries (e.g. maleimide-thiol coupling) is the limited control over the site of conjugation in cases where multiple reactive functionalities are present, leading to heterogeneous products and in some cases dysfunctional conjugates. Bioorthogonal coupling approaches such as the well-established copper-catalyzed azide-alkyne cycloaddition (CuAAC) "click" reaction are attractive alternatives as the reaction kinetics are favorable and azide-containing reagents are widely available. In the work described here, we prepared lipids containing a reactive cyclooctyne group and, after incorporation into liposomes, demonstrated successful conjugation of both a small molecule dye (5′-TAMRA-azide) as well as a larger azide-containing model protein based upon a designed ankyrin repeat protein (azido-DARPin). By applying the strain-promoted azido-alkyne cycloaddition (SPAAC) the use of Cu(I) as a catalyst is avoided, an important advantage considering the known deleterious effects associated with copper in cell and protein studies. We demonstrate complete control over the number of ligands coupled per liposome when using a small molecule azide with conjugation occurring at a reasonable reaction rate. By comparison, the conjugation of a larger azide-modified protein occurs more slowly, however the number of protein ligands coupled was found to be sufficient for liposome targeting to cells. Importantly, these results provide a strong proof of concept for the site-specific conjugation of protein ligands to liposomal surfaces via SPAAC. Unlike conventional approaches, this strategy provides for the homogeneous coupling of proteins bearing a single site-specific azide modification and eliminates the chance of forming dysfunctional ligands on the liposome. Furthermore, the absence of copper in the reaction process should also make this approach much more compatible with cell-based and in vivo applications

CCDC 1999456: Experimental Crystal Structure Determination

Related Article: Charalampos G. Pappas, Pradeep K. Mandal, Bin Liu, Brice Kauffmann, Xiaoming Miao, Dávid Komáromy, Waldemar Hoffmann, Christian Manz, Rayoon Chang, Kai Liu, Kevin Pagel, Ivan Huc, Sijbren Otto|2020|Nature Chemistry|12|1180|doi:10.1038/s41557-020-00565-

CCDC 1575884: Experimental Crystal Structure Determination

Related Article: Tjie Kok, Hannah Wapenaar, Kan Wang, Constantinos G. Neochoritis, Tryfon Zarganes-Tzitzikas, Giordano Proietti, Nikolaos Eleftheriadis, Katarzyna Kurpiewska, Justyna Kalinowska-Tłuścik, Robbert H. Cool, Gerrit J. Poelarends, Alexander Dömling, Frank J. Dekker|2018|Bioorg.Med.Chem.|26|999|doi:10.1016/j.bmc.2017.12.032,An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.

CCDC 1942977: Experimental Crystal Structure Determination

Related Article: Charalampos G. Pappas, Pradeep K. Mandal, Bin Liu, Brice Kauffmann, Xiaoming Miao, Dávid Komáromy, Waldemar Hoffmann, Christian Manz, Rayoon Chang, Kai Liu, Kevin Pagel, Ivan Huc, Sijbren Otto|2020|Nature Chemistry|12|1180|doi:10.1038/s41557-020-00565-

CCDC 764607: Experimental Crystal Structure Determination

Related Article: T.Jerphagnon, A.J.A.Gayet, F.Berthiol, V.Ritleng, N.Mrsic, A.Meetsma, M.Pfeffer, A.J.Minnaard, B.L.Feringa, J.G.de Vries|2009|Chem.-Eur.J.|15|12780|doi:10.1002/chem.200902103,An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.