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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
Published on: March 6, 2013
Synthesis, crystal structure and studies on the interaction with albumin of a new silver(I) complex based on
Lucius Flavius Ourives Bomfim Filho1, Cleidivania Rocha1, Bernardo Lages Rodrigues1
1Chemistry Department, Universidade Federal de Minas Gerais, 31270-901 Belo Horizonte, Minas Gerais, Brazil.
Abstract:
In the present work, the two-dimensional (2D) polymer poly[[μ4-2-(4-nitrobenzenesulfonamido)benzoato-κ4O1:O1:O1':N6]silver(I)] (AgL), [Ag(C13H9N2O6S)]n, was obtained from 2-(4-nitrobenzenesulfonamido)benzoic acid (HL), C13H10N2O6S. FT-IR, 1H and 13C{1H} NMR spectroscopic analyses were used to characterize both compounds. The crystal structures of HL and AgL were determined by single-crystal X-ray diffraction. In the structure of HL, O-H...O hydrogen bonds between neighbouring molecules result in the formation of dimers, while the silver(I) complex shows polymerization associated with the O atoms of three distinct deprotonated ligands (L-). Thus, the structure of the Ag complex can be considered as a coordination polymer consisting of a one-dimensional linear chain, constructed by carboxylate bridging groups, running parallel to the b axis. Neighbouring polymeric chains are further bridged by Ag-C monohapto contacts, resulting in a 2D framework. Fingerprint analysis of the Hirshfeld surfaces show that O...H/H...O hydrogen bonds are responsible for the most significant contacts in the crystal packing of HL and AgL, followed by the H...H and O...C/C...O interactions. The Ag...Ag, Ag...O/O...Ag and Ag...C/C...Ag interactions in the Hirshfeld surface represent 12.1% of the total interactions in the crystal packing. Studies of the interactions of the compounds with human serum albumin (HSA) indicated that both HL and AgL interact with HSA.
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