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Synthesis, crystal structure and studies on the interaction with albumin of a new silver(I) complex based on 2‐(4‐nitrobenzenesulfonamido)benzoic acid
Author(s) -
Bomfim Filho Lucius Flavius Ourives,
Rocha Cleidivania,
Rodrigues Bernardo Lages,
Beraldo Heloisa,
Teixeira Leticia Regina
Publication year - 2019
Publication title -
acta crystallographica section c
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.304
H-Index - 17
ISSN - 2053-2296
DOI - 10.1107/s2053229619008593
Subject(s) - crystallography , hydrogen bond , carboxylate , crystal structure , deprotonation , chemistry , benzoic acid , molecule , monomer , single crystal , polymer , stereochemistry , ion , organic chemistry
In the present work, the two‐dimensional (2D) polymer poly[[μ 4 ‐2‐(4‐nitrobenzenesulfonamido)benzoato‐κ 4 O 1 : O 1 : O 1′ : N 6 ]silver(I)] (Ag L ), [Ag(C 13 H 9 N 2 O 6 S)] n , was obtained from 2‐(4‐nitrobenzenesulfonamido)benzoic acid (H L ), C 13 H 10 N 2 O 6 S. FT–IR, 1 H and 13 C{ 1 H} NMR spectroscopic analyses were used to characterize both compounds. The crystal structures of H L and Ag L were determined by single‐crystal X‐ray diffraction. In the structure of H L , 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 H L and Ag L , 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 H L and Ag L interact with HSA.