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PubMed2002

Study of Cd2+ complexation by the glutathione fragments Cys-Gly (CG) and gamma-Glu-Cys (gamma-EC) by differential pulse polarography.

A differential pulse polarographic study of the Cd2+/gamma-Glu-Cys and Cd2+/Cys-Gly systems assisted by the alternating least-squares multivariate curve resolution (MCR-ALS) method was carried out to obtain a better understanding of the different metal affinities of the complexation sites on glutathione (GSH). The simultaneous analysis of the titration of peptide with metal and of metal with peptide allowed the resolution of the Cd2+/Cys-Gly system, whereas in the analysis of the Cd2+/gamma-Glu-Cys system the analysis of a single titration experiment was sufficient. The analysis of the shape of the resulting pure voltammograms and concentration profiles of the resolved components suggested the presence of two different types of bound Cd2+ in the two systems considered, that could be attributed to Cd2+ bound to one or two sulfur atoms to form complexes of stoichiometry 1:1 and 1:2. respectively.

Journal Article↗

PubMed2003

An all-atom solution-equilibrated model for human extrinsic blood coagulation complex (sTF-VIIa-Xa): a protein-protein docking and molecular dynamics refinement study.

Tissue factor (TF)-bound factor (F)VIIa plays a critical role in activating FX, an event that rapidly results in blood coagulation. Despite recent advances in the structural information about soluble TF (sTF)-bound VIIa and Xa individually, the atomic details of the ternary complex are not known. As part of our long-term goal to provide a structural understanding of the extrinsic blood coagulation pathway, we built an all atom solution-equilibrated model of the human sTF-VIIa-Xa ternary complex using protein-protein docking and molecular dynamics (MD) simulations. The starting structural coordinates of sTF-VIIa and Xa were derived from dynamically equilibrated solution structures. Due to the flexible nature of the light-chain of the Xa molecule, a three-stage docking approach was employed in which SP (Arg195-Lys448)/EGF2 (Arg86-Arg139), EGF1 (Asp46-Thr85) and GLA (Ala1-Lys45) domains were docked in a sequential manner. The rigid-body docking approach of the FTDOCK method in conjunction with filtering based on biochemical knowledge from experimental site-specific mutagenesis studies provided the strategy. The best complex obtained from the docking experiments was further refined using MD simulations for 3 ns in explicit water. In addition to explaining most of the known experimental site-specific mutagenesis data pertaining to sTF-VIIa, our model also characterizes likely enzyme-binding exosites on FVIIa and Xa that may be involved in the ternary complex formation. According to the equilibrated model, the 140s loop of VIIa serves as the key recognition motif for complex formation. Stable interactions occur between the FVIIa 140s loop and the FXa -strand B2 region near the sodium-binding domain, the 160 s loop and the N-terminal activation loop regions. The helical-hydrophobic stack region that connects the GLA and EGF1 domains of VIIa and Xa appears to play a potential role in the membrane binding region of the ternary complex. The proposed model may serve as a reasonable structural basis for understanding the exosite-mediated substrate recognition of sTF-VIIa and to advance understanding of the TFPI-mediated regulatory pathway of the extrinsic blood coagulation cascade.

Binding Sites↗

PubMed2000

Structural and functional features of the Escherichia coli F1-ATPase.

The structural organization and overall dimensions of the Escherichia coli F1-ATPase in solution has been analyzed by synchroton X-ray scattering. Using an independent ab initio approach, the low-resolution shape of the hydrated enzyme was determined at 3.2 nm resolution. The shape permitted unequivocal identification of the volume occupied by the alpha3beta3gamma complex of the atomic model of the ECF1-ATPase. The position of the delta and epsilon subunits were found by interactive fitting of the solution scattering data and by cross-linking studies. Laser-induced covalent incorporation of 2-azido-ATP established a direct relationship between nucleotide binding affinity and the different interactions between the stalk subunits gamma and epsilon with the three catalytic subunits (beta) of the F1-ATPase. Mutants of the ECF1-ATPase with the introduction of Trp-for-Tyr replacement in the catalytic site of the complex made it possible to monitor the activated state for ATP synthesis (ATP conformation) in which the gamma and epsilon subunits are in close proximity to the alpha subunits and the ADP conformation, with the stalk subunits are linked to the beta subunit.

Escherichia coli↗

PubMed2003

Interactions between synaptic vesicle fusion proteins explored by atomic force microscopy.

Measuring the biophysical properties of macromolecular complexes at work is a major challenge of modern biology. The protein complex composed of vesicle-associated membrane protein 2, synaptosomal-associated protein of 25 kDa, and syntaxin 1 [soluble N-ethyl-maleimide-sensitive factor attachment protein receptor (SNARE) complex] is essential for docking and fusion of neurotransmitter-filled synaptic vesicles with the presynaptic membrane. To better understand the fusion mechanisms, we reconstituted the synaptic SNARE complex in the imaging chamber of an atomic force microscope and measured the interaction forces between its components. Each protein was tested against the two others, taken either individually or as binary complexes. This approach allowed us to determine specific interaction forces and dissociation kinetics of the SNAREs and led us to propose a sequence of interactions. A theoretical model based on our measurements suggests that a minimum of four complexes is probably necessary for fusion to occur. We also showed that the regulatory protein neuronal Sec1 injected into the atomic force microscope chamber prevented the complex formation. Finally, we measured the effect of tetanus toxin protease on the SNARE complex and its activity by on-line registration during tetanus toxin injection. These experiments provide a basis for the functional study of protein microdomains and also suggest opportunities for sensitive screening of drugs that can modulate protein-protein interactions.

Antigens, Surface↗

PubMed2006

Chitosan-mediated synthesis of gold nanoparticles by UV photoactivation and their characterization.

Recent researches have largely been focused on chitosan, which is deacetylated chitin, the most abundant natural polysaccharide after cellulose. In this paper, we report the fabrication of gold nanoparticles (GNPs) by UV photoactivation in the presence of biopolymeric chitosan and the tracing of the gold salt solution aging. Detailed UV-visible spectroscopy study witnessed the evolution of the surface plasmon resonance (SPR) adsorption during the GNP growth. The effect of chitosan in aqueous solution for the GNP preparation was investigated in detail. The results indicated the size and distribution of GNPs could be controlled over by altering the concentration of chitosan, and the GNP growth during aging was a chitosan-mediated autocatalytic process. Fourier transform infrared spectroscopy (FTIR) showed the hydroxyl in molecular chitosan was oxidized to carbonyl groups in the fabrication of GNPs after aging and nitrogen atoms are the main sites for the complexation of chitosan with Au atoms. Our synthesis method in the present way can be used to form self-assemble monolayers of GNPs and fabricate biosensors based on surface plasmon resonance effect.

Adsorption↗

PubMed2003

X-ray structure of the cyclomaltohexaicosaose triiodide inclusion complex provides a model for amylose-iodine at atomic resolution.

Cyclomaltohexaicosaose (CA26) is folded into two 1(2)/(3) turns long V-helices that are oriented antiparallel. Crystals of complexes of CA26 with NH(4)I(3) and Ba(I(3))(2) are brown and X-ray analyses show that I(3)(-) units are located in the approximately 5 A wide central channels of the V-helices. In the complex with NH(4)I(3), two CA26 molecules are stacked to form 2 x 1(2)/(3) turns long channels harbouring 3 I(3)(-) at 3.66-3.85 A inter I(3)(-) distance (shorter than van der Waals distance, 4.3 A), whereas in the Ba(I(3))(2) complex, CA26 are not stacked and only one I(3)(-) each fills the V-helices. Glucose...I contacts are formed with C5-H, C3-H, C6-H and (at the ends of the V-helices) with O6 in (+) gauche orientation. By contrast, O2, O3, O4 and O6 in the preferred (-) gauche orientation do not interact with I because these distances are >/=4.01 A and exceed the van der Waals I...O sum of radii by about 0.5 A except for one O2...I distance of 3.68 A near the end of one V-helix. Raman spectra indicate that the complexes share the presence of I(3)(-) with blue amylose-iodine.

Amylose↗

PubMed1997

Barley lipid-transfer protein complexed with palmitoyl CoA: the structure reveals a hydrophobic binding site that can expand to fit both large and small lipid-like ligands.

BACKGROUND: . Plant nonspecific lipid-transfer proteins (nsLTPs) bind a variety of very different lipids in vitro, including phospholipids, glycolipids, fatty acids and acyl coenzyme As. In this study we have determined the structure of a nsLTP complexed with palmitoyl coenzyme A (PCoA) in order to further our understanding of the structural mechanism of the broad specificity of these proteins and its relation to the function of nsLTPs in vivo. RESULTS: . 1H and 13C nuclear magnetic resonance spectroscopy (NMR) have been used to study the complex between a nsLTP isolated from barley seeds (bLTP) and the ligand PCoA. The resonances of 97% of the 1H atoms were assigned for the complexed bLTP and nearly all of the resonances were assigned in the bound PCoA ligand. The palmitoyl chain of the ligand was uniformly 13C-labelled allowing the two ends of the hydrocarbon chain to be assigned. The comparison of a subset of 20 calculated structures to an average structure showed root mean square deviations of 1.89 +/- 0.19 for all C, N, O, P and S atoms of the entire complex and of 0.57 +/- 0.09 for the peptide backbone atoms of the four alpha helices of the complexed bLTP. The four-helix topology of the uncomplexed bLTP is maintained in the complexed form of the protein. The bLTP only binds the hydrophobic parts of PCoA with the rest of the ligand remaining exposed to the solvent. The palmitoyl chain moiety of the ligand is placed in the interior of the protein and bent in a U-shape. This part of the ligand is completely buried within a hydrophobic pocket of the protein. CONCLUSIONS: . A comparison of the structures of bLTP in the free and bound forms suggests that bLTP can accommodate long olefinic ligands by expansion of the hydrophobic binding site. This expansion is achieved by a bend of one helix, HA, and by conformational changes in both the C terminus and helix HC. This mode of binding is different from that seen in the structure of maize nsLTP in complex with palmitic acid, where binding of the ligand is not associated with structural changes.

Amino Acid Sequence↗

PubMed2004

Tetraaqua(3,4,7,8-tetramethyl-1,10-phenanthroline-kappa2N,N')zinc(II) thiosulfate.

In the title complex of zinc(II) with 3,4,7,8-tetramethyl-1,10-phenanthroline (tmph), viz. [Zn(C16H16N2)(H2O)4](S2O3), the metal atom has a monomeric octahedral ZnN2O4 complex environment comprising two N-atom donors from the tmph group and four aqua O-atom donors. The complex cation is connected to four thiosulfate anions through a compact hydrogen-bonding network involving all coordinated aqua H-atom donors and all the outer acceptors (O and S) of the anion.

Anti-Inflammatory Agents, Non-Steroidal↗

PubMed2004

On the noble-gas-induced intersystem crossing for the CUO molecule: experimental and theoretical investigations of CUO(Ng)n (Ng = Ar, Kr, Xe; n = 1, 2, 3, 4) complexes in solid neon.

Uranium atoms excited by laser ablation react with CO in excess neon to produce the novel CUO molecule, which forms distinct Ng complexes (Ng = Ar, Kr, Xe) when the heavier noble gases are added. The CUO(Ng) complexes are identified through CO isotopic and Ng substitution on the neon matrix infrared spectra and by comparison to DFT frequency calculations. The U-C and U-O stretching frequencies of CUO(Ng) complexes are slightly red-shifted from frequencies for the (1)Sigma(+) CUO ground state, which identifies singlet ground state CUO(Ng) complexes. In solid neon the CUO molecule is also a complex CUO(Ne)(n), and the CUO(Ne)(n-1)(Ng) complexes are likewise specified. The next singlet CUO(Ne)(x)(Ng)(2) complexes in excess neon follow in like manner. However, the higher CUO(Ne)(x)(Ng)(n) complex (n = 3, 4) stretching modes approach pure argon matrix CUO(Ar)(n) values and isotopic behavior, which are characterized as triplet ground state complexes by DFT frequency calculations. This work suggests that the singlet-triplet crossing occurs with 3 Ar, 3 Kr, or 4 Xe and a balance of Ne atoms coordinated to CUO in the neon matrix host.

Journal Article↗

PubMed1994

Three-dimensional 1H NMR structure of the nucleocapsid protein NCp10 of Moloney murine leukemia virus.

The nucleocapsid protein of Moloney murine leukemia virus (NCp10) is a 56-amino acid protein which contains one zinc finger of the CysX2CysX4HisX4Cys form, a highly conserved motif present in most retroviruses and retroelements. At pH > or = 5, NCp10 binds one zinc atom and the complexation induces a folding of the CysX2CysX4HEsX4Cys box, similar to that observed for the zinc-binding domains of HIV-1 NC protein. The three-dimensional structure of NCp10 has been determined in aqueous solution by 600 MHz 1H NMR spectroscopy. The proton resonances could be almost completely assigned by means of phase-sensitive double-quantum-filtered COSY, TOCSY and NOESY techniques. NOESY spectra yielded 597 relevant structural constraints, which were used as input for distance geometry calculations with DIANA. Further refinement was performed by minimization with the program AMBER, which was modified by introducing a zinc force field. The solution structure is characterized by a well-defined central zinc finger (rmsd of 0.747 +/- 0.209 A for backbone atoms and 1.709 +/- 0.187 A when all atoms are considered), surrounded by flexible N- and C-terminal domains. The Tyr28, Trp35, Lys37, Lys41 and Lys42 residues, which are essential for activity, lie on the same face of the zinc finger, forming a bulge structure probably involved in viral RNA binding. The significance of these structural characteristics for the various biological functions of the protein is discussed, taking into account the results obtained with various mutants.

Amino Acid Sequence↗

PubMed2004

Two series of novel rare earth complexes with dicyanamide [Ln(dca)2(phen)2(H2O)3][dca].(phen), (Ln = Pr, Gd, and Sm) and [Ln(dca)3(2,2'-bipy)2(H2O)]n, (Ln = Gd, Sm, and La): syntheses, crystal structures, and magnetic properties.

Two series of novel complexes, [Ln(dca)(2)(Phen)(2)(H(2)O)(3)](dca).(phen) (Ln = Pr (1), Gd (2), and Sm (3), dca = N(CN)(-), phen = 1,10-phenanthroline) and [Ln(dca)(3)(2,2'-bipy)(2)(H(2)O)](n), (Ln = Gd (4), Sm (5), and La (6), 2,2'-bipy = 2,2'-bipydine), have been synthesized and structurally characterized by X-ray crystallography. The crystal structures of the first series (1-3) are isomorphous and consist of discrete [Ln(dca)(2)(Phen)(2)(H(2)O)(3)]+ cations, dca anions, and lattice phen molecules; whereas the structures of the second series (4-6) are characterized by infinite chains [Ln(dca)(3)(2,2'-bipy)(2)(H(2)O)](n). The Ln(III) atoms in all complexes are nine-coordinated and form a distorted tricapped trigonal prism environment. The three-dimensional frameworks of 1-6 are constructed by intermolecular hydrogen bond interactions. Variable-temperature magnetic susceptibility measurements for complexes 1, 2, 4, and 5 indicate a Curie-Weiss paramagnetic behavior over 5-300 K.

Journal Article↗

PubMed2004

Arsenic availability, toxicity and direct role of GSH and phytochelatins in As detoxification in the green alga Stichococcus bacillaris.

Accumulation and toxicity of inorganic arsenic forms As(III) and As(V) to the green microalga Stichococcus bacillaris depended on environmental variables. pH of exposure and to a lesser extent elevated concentrations of humic acid, chloride and orthophosphate ions affected arsenic accumulation and its toxicity. As(V) was more toxic than As(III), especially at the near neutral pH 6.8. Intracellular As(V) uptake by algal cells was greater at pH 6.8 than at 8.2. In response to As(III) and As(V) the alga produced phytochelatins (PC(2-3)), but at As(V) exposure, their levels in cells were higher than with As(III), suggesting higher As(V) than As(III) availability and uptake. Arsenic in algal cells occurred in various complexes with non-protein SH groups. Some of these complexes dissociated under acidic conditions, but others were able to dissociate only at an alkaline pH. The former consisted of SH groups of phytochelatins. Those dissociating at an alkaline pH involved SH groups from both glutathione (GSH) and phytochelatins (PC) or their derivatives. In the predominant acid-stable mixed As-SH complex, the ratio of SH (PC(2)) to SH (GSH) was 2:1, which suggests that one molecule of PC(2) (containing two SH groups) together with one molecule of GSH were involved in intracellular complexation of each As atom. This is the first demonstration of GSH involvement in arsenic complexation, in vivo. The intracellular concentration of As was greater than that of non-protein SH groups which suggests that not all the arsenic in algal cells was complexed and detoxified by thiol groups.

Arsenic↗

PubMed2001

Substitution and oxidation reactions of bis(dithiolene)tungsten complexes of potential relevance to enzyme sites.

Structurally characterized tungstoenzymes contain mononuclear active sites in which tungsten is coordinated by two pterin-dithiolene ligands and one or two additional ligands that have not been identified. In this and prior investigations (Sung, K.-M.; Holm, R. H. Inorg. Chem. 2000, 39, 1275; J. Am. Chem. Soc. 2001, 123, 1931), stable coordination units of bis(dithiolene)tungsten(IV,V,VI) complexes potentially related to enzyme sites have been sought by exploratory synthesis. In this work, additional members of the sets [WL(S2C2Me2)2](2-,-) and [WLL'(S2C2Me2)2](2-,-) have been prepared and structurally characterized. Tungsten(IV) complexes obtained by substitution are carbonyl displacement products of [W(CO)2(S2C2Me2)2] and include those with the groups W(IV)S (4), W(IV)(O2CPh) (5), and W(IV)(2-AdQ)(CO) (Q = S (6), Se (7); Ad = adamantyl). Those obtained by oxidation reactions contain the groups W(V)O (9), W(V)(QPh)2 (Q = S (10), Se (11)), W(VI)S(OPh) (12), and W(VI)O2 (14). The latter two complexes were obtained from W(IV) precursors using sulfur and oxygen atom transfer reactions, respectively. Complexes 4 and 9 are square pyramidal; 6, 7, 10, and 11 are distorted trigonal prismatic with cis ligands LL'; and 12 and 14 are distorted octahedral. Complexes 4, 10, and 11 support three-membered electron transfer series. Attempts to oxidize 4 to the W(V)S complex results in the formation of binuclear [W2(mu2-S)2(S2C2Me2)4](2-) having distorted octahedral coordination. The 21 known functional groups WL and WLL' in mononuclear bis(dithiolene) complexes prepared in this and prior investigations are tabulated. Of those with physiological-type ligands, it remains to be seen which (if any) of these ligation modes are displayed by enzyme sites.

Catalytic Domain↗

PubMed2005

An all atom energy based computational protocol for predicting binding affinities of protein-ligand complexes.

We report here a computationally fast protocol for predicting binding affinities of non-metallo protein-ligand complexes. The protocol builds in an all atom energy based empirical scoring function comprising electrostatics, van der Waals, hydrophobicity and loss of conformational entropy of protein side chains upon ligand binding. The method is designed to ensure transferability across diverse systems and has been validated on a heterogenous dataset of 161 complexes consisting of 55 unique protein targets. The scoring function trained on a dataset of 61 complexes yielded a correlation of r=0.92 for the predicted binding free energies against the experimental binding affinities. Model validation and parameter analysis studies ensure the predictive ability of the scoring function. When tested on the remaining 100 protein-ligand complexes a correlation of r=0.92 was recovered. The high correlation obtained underscores the potential applicability of the methodology in drug design endeavors. The scoring function has been web enabled at as binding affinity prediction of protein-ligand (BAPPL) server.

Drug Design↗

PubMed2001

Polymeric[mu(3)-(N-phosphonomethyl)-glycinato]tris(tri-n-butyltin).

N-(Phosphonomethyl)glycine, glyphosate, reacts with bis(tributyltin) oxide to form a ligand--tin (1:3) complex in which all five O atoms are coordinated to tin. The complex, [Sn(3)(C(4)H(9))(9)(C(3)H(5)NO(5)P)], is polymeric, with the glyphosate and two tributyltin groups forming a two-dimensional network and with the third Sn atom alternately above and below the plane of the net. The Sn atoms in the network have a trigonal-bipyramidal coordination, with O atoms in the axial positions and C atoms in the equatorial positions; the pendant tributyltin group is tetrahedrally coordinated to one O atom and to three butyl groups. Sn--O distances vary from 2.030 (3) to 2.408 (3) A. The Sn--O distances for O atoms trans to carboxylate groups are shorter than those trans to phosphonate groups and d(Sn--O) decreases with increasing d(C/P--O) (Delta(Sn--O) approximately -4.6 Delta(C/P--O)). The amino N atom in the ligand is neither protonated nor involved in coordination to the Sn atoms.

Crystallography, X-Ray↗

PubMedDate not supplied

Copper and zinc speciation in the solution of a soil-sludge mixture.

Only a small fraction of the transition metals content in sludge-amended soils is soluble, and yet this fraction is a major contributor to the mobility and bioavailability of the metals. The chemical species of zinc (Zn) and copper (Cu) in the soluble fractions of soil-sludge mixtures were characterized with respect to their charge, molecular weight, and stoichiometry using ion exchange resin and gel chromatography procedures. The change in the metals' species with time after sludge application was followed for 100 d. Copper in the water extracts of the sludge-sand mixtures was found almost exclusively in low molecular weight (below 1000 Da) complexes. Higher molecular weight (around 2500 Da) dissolved organic carbon (DOC) was present in the extracts as well, but this DOC fraction exhibited little complexation. Copper was present in the extracts mainly as negatively charged species throughout the incubation period, and zinc tended to form zwitter ions. As incubation progressed, the relative content of positively charged Zn in solution increased. Complexation capacity of DOC in sludge water extract, extrapolated to infinite dilution, was 8.75 mM Ca g(-1) DOC. When the complexation capacity of the extract is near saturation, a mean Cu-DOC complex can be defined. It consists of 1.9 Cu atoms attached to DOC species containing 5.6 C atoms. Thus, the organic Cu complexes consist primarily of about two Cu ions attached to DOC species containing only five or six C atoms. Amino acids and small peptides or polycarboxylic acids, such as citric acid, thus may be important complexing agents of the metal.

Amino Acids↗

PubMed1988

Integral complexes of cytochrome c oxidase contain three coppers.

Metal contents have been determined in beef heart cytochrome c oxidase by inductively coupled plasma atomic emission spectroscopy. Integral complexes of this enzyme contain three copper and two iron atoms, as well as one zinc and one magnesium atom (Cu: 2, 91 +/- 0, 13; Fe: 2, 05 +/- 0, 17; Zn: 1, 03 +/- 0, 03; Mg: 1, 01 +/- 0, 10). The combination of these results with those reported for the c1 aa3-oxidase from Thermus thermophilus leads to the conclusion that subunit I is the universal two coppers and two hemes a binding catalytic unit common to all oxidases of the aa3-type. Subunit II, which binds the third copper ion, functions as an electron conducting unit, transferring electrons from cytochrome c to the four redox centers in subunit I. Preliminary titration experiments with NADH reveal, in agreement with this catalytic organisation, the presence of five redox centers.

Amino Acids↗

PubMed2000

Formation of mono-, bi-, tri-, and tetranuclear Ag(I) complexes of C3-symmetric tripodal benzimidazole ligands.

The C3-symmetric tripodal ligand tris(2-benzimidazolylmethyl)amine (ntb) and its alkyl-substituted derivatives tris(N-R-benzimidazol-2-ylmethyl)amine (R = methyl, Mentb; R = ethyl, Etntb; R = propyl, Prntb) react with various silver(I) salts to afford mononuclear [Ag(Prntb)(CF3SO3)].0.25H2O, 1, binuclear [Ag2(Mentb)2](CF3SO3)2.H2O, 2, trinuclear [Ag3(Etntb)2](ClO4)3.CH3OH, 3, and tetranuclear [Ag4(ntb)2(CH3CN)2(CF3CO2)2](CF3CO2)2.2H2O, 4. All four complexes have been characterized by elemental analyses, IR spectroscopy, and X-ray crystallography. The Ag(I) ion in 1 is coordinated to the three imine nitrogen atoms of the Prntb ligand and one oxygen atom of the trifluoromethanesulfonate anion in a distorted tetrahedral environment. Dinuclear 2 has C2 symmetry with each Ag(I) atom trigonally coordinated by two arms of one Mentb and one arm of another. Trinuclear 3 has C3 symmetry with a Ag3 regular triangle sandwiched between a pair of Etntb ligands such that one arm of each ligand is involved in linear coordination about an Ag(I) atom. In the tetranuclear complex 4, two linearly coordinated Ag(I) atoms lying on the molecular C2 axis are bridged by a pair of ntb ligands and the remaining pendant arm of each ntb ligand is attached to another Ag(I) atom whose tetrahedral coordination sphere is completed by an acetonitrile molecule and a chelating trifluoroacetate anion. Complexes 2 and 3 may be regarded as an aggregation of two tridentate ligands by a silver dimer and a trinuclear cluster with weak Ag...Ag interactions, respectively, while in 4 the aggregation of two tripodal ligands by four Ag(I) ions affords a multicomponent internal cavity. The packing modes of complexes 1-3 are dominated by weak supramolecular pi...pi and CH...pi interactions. Hexagonal or square channels are generated in 1 and 2, and a honeycomb layer structure is formed in 3 with solvate molecules and counteranions occupying the voids. The crystal structure of 4 consists of a three-dimensional network consolidated by NH...O and OH...O hydrogen bonds.

Journal Article↗