Small-angle x-ray scattering study of the aggregation of gold nanoparticles during formation at the toluene-water interface

We report the results of an in situ small-angle x-ray scattering (SAXS) study of the aggregation of gold nanoparticles formed by an interfacial reaction at the toluene-water interface. The SAXS data provide a direct evidence for aggregate formation of nanoparticles having 1.3 nm gold core and an organic shell that gives a core-core separation of about 2.5 nm. Furthermore, the nanoparticles do not occupy all the cites of 13-member cluster. This occupancy decreases with reaction time and indicate reorganization of the clusters that generates planner disklike structures. A gradual increase in fractal dimension from 1.82 to 2.05 also indicate compactification of cluster aggregation with reaction time, the final exponent being close to 2 expected for disklike aggregates.

Aggregation studies in crystals of apolar helical peptides: Boc-Aib-Val-Ala-Leu-Aib-Val-Ala-Leu-Aib-OMe

In the crystal, the backbone of Boc-(Aib-Val-Ala-Leu)2-Aib-OMe adopts a helical form with four alpha-type hydrogen bonds in the middle, flanked by 3(10)-type hydrogen bonds at either end. The helical molecules stack in columns with head-to-tail hydrogen bonds, either directly between NH and CO, or bridged by solvent molecules. The packing of the helices is parallel, even in space group P2(1). Cell parameters are a = 9.837(2) A, b = 15.565(3) A, c = 20.087(5) A, beta = 96.42(2) degrees, dcalc = 1.091 g/cm3 for C46H83N9O12.1.5H2O.0.67CH3OH. There appears to be some hydration of the backbone in this apolar helix.

Parallel and antiparallel aggregation of alpha-helices. Crystal structures of two apolar decapeptides X-Trp-Ile-Ala-Aib-Ile-Val-Aib-Leu-Aib-Pro-OMe (X = Boc, Ac)

An apolar helical decapeptide with different end groups, Boc- or Ac-, crystallizes in a completely parallel fashion for the Boc-analog and in an antiparallel fashion for the Ac-analog. In both crystals, the packing motif consists of rows of parallel molecules. In the Boc-crystals, adjacent rows assemble with the helix axes pointed in the same direction. In the Ac-crystals, adjacent rows assemble with the helix axes pointed in opposite directions. The conformations of the molecules in both crystals are quite similar, predominantly alpha-helical, except for the tryptophanyl side chain where chi 1 congruent to 60 degrees in the Boc- analog and congruent to 180 degrees in the Ac-analog. As a result, there is one lateral hydrogen bond between helices, N(1 epsilon)...O(7), in the Ac-analog. The structures do not provide a ready rationalization of packing preference in terms of side-chain interactions and do not support a major role for helix dipole interactions in determining helix orientation in crystals. The crystal parameters are as follow. Boc-analog: C60H97N11O13.C3H7OH, space group Pl with a = 10.250(3) A, b = 12.451(4) A, c = 15.077(6) A, alpha = 96.55(3) degrees, beta = 92.31(3) degrees, gamma = 106.37(3) degrees, Z = 1, R = 5.5% for 5581 data ([F] greater than 3.0 sigma(F)), resolution 0.89 A. Ac-analog: C57H91N11O12, space group P2(1) with a = 9.965(1) A, b = 19.707(3) A, c = 16.648(3) A, beta = 94.08(1), Z = 2, R = 7.2% for 2530 data ([F] greater than 3.0 sigma(F)), resolution 1.00 A.

Aggregation and mesomorphic properties of 'double-headed' carbohydrate amphiphiles

Sugar-based amphiphiles, consisting of two sugar head groups and an alkylene chain within the molecules, are synthesized and their aggregation and mesomorphic properties are evaluated. The hydrophilic sugar head groups, constituted with beta-D-glucopyranoside units, and the lyophilic alkylene units, are coupled to a glycerol backbone to afford the 'double-headed' sugar amphiphiles. Aggregation studies in aqueous solutions provided their critical micellar concentrations and the aggregation numbers. Mesophase characterizations by polarizing optical microscopy and differential scanning calorimetry (DSC) revealed the phase-transition behaviour of these new 'double-headed' glycolipids.

Covalent tethering of the dimer interface annuls aggregation in thymidylate synthase

Thymidylate synthase (TS), a dimeric enzyme, forms large soluble aggregates at concentrations of urea (3.3-5 M), well below that required for complete denaturation, as established by fluorescence and size-exclusion chromatography. In contrast to the wild-type enzyme, an engineered mutant of TS (T155C/E188C/C244T), TSMox, in which two subunits are crosslinked by disulfide bridges between residues 155-188' and 188-155', does not show this behavior. Aggregation behavior is restored upon disulfide bond reduction in the mutant protein, indicating the involvement of interface segments in forming soluble associated species. Intermolecular disulfide crosslinking has been used as a probe to investigate the formation of larger non-native aggregates. The studies argue for the formation of large multimeric species via a sticky patch of polypeptide from the dimer interface region that becomes exposed on partial unfolding. Covalent reinforcement of relatively fragile protein-protein interfaces may be a useful strategy in minimizing aggregation of non-native structures in multimeric proteins.

Synthesis, aggregation behavior and cholesterol solubilization studies of 16-epi-pythocholic acid (3 alpha,12 alpha,16 beta-trihydroxy-5 beta-cholan-24-oic acid)

Synthesis, aggregation behavior and in vitro cholesterol solubilization studies of 16-epi-pythocholic acid (3 alpha,12 alpha,16 beta-trihydroxy-5 beta-cholan-24-oic acid, EPCA) are reported. The synthesis of this unnatural epimer of pythocholic acid (3 alpha,12 alpha,16 alpha-trihydroxy-5 beta-cholan-24-oic acid, PCA) involves a series of simple and selective chemical transformations with an overall yield of 21% starting from readily available cholic acid (CA). The critical micellar concentration (CMC) of 16-epi-pythocholate in aqueous media was determined using pyrene as a fluorescent probe. In vitro cholesterol solubilization ability was evaluated using anhydrous cholesterol and results were compared with those of other natural di-and trihydroxy bile acids. These studies showed that 16-epi-pythocholic acid (16 beta-hydroxy-deoxycholic acid) behaves similar to cholic acid (CA) and avicholic acid (3 alpha,7 alpha,16 alpha-trihydroxy-5 beta-cholan-24-oic acid, ACA) in its aggregation behavior and cholesterol dissolution properties. (C) 2010 Elsevier Inc. All rights reserved.

Design of incentive compatible protocols for wireless networks: A game theoretic approach

In this thesis work, we design rigorous and efficient protocols/mechanisms for different types of wireless networks using a mechanism design [1] and game theoretic approach [2]. Our work can broadly be viewed in two parts. In the first part, we concentrate on ad hoc wireless networks [3] and [4]. In particular, we consider broadcast in these networks where each node is owned by independent and selfish users. Being selfish, these nodes do not forward the broadcast packets. All existing protocols for broadcast assume that nodes forward the transit packets. So, there is need for developing new broadcast protocols to overcome node selfishness. In our paper [5], we develop a strategy proof pricing mechanism which we call immediate predecessor node pricing mechanism (IPNPM) and an efficient new broadcast protocol based on IPNPM. We show the efficacy of our proposed broadcast protocol using simulation results.

An auction algorithm for procuring wireless channel in a heterogenous wireless network

In this paper, we develop a novel auction algorithm for procuring wireless channel by a wireless node in a heterogeneous wireless network. We assume that the service providers of the heterogeneous wireless network are selfish and non-cooperative in the sense that they are only interested in maximizing their own utilities. The wireless user needs to procure wireless channels to execute multiple tasks. To solve the problem of the wireless user, we propose a reverse optimal (REVOPT) auction and derive an expression for the expected payment by the wireless user. The proposed auction mechanism REVOPT satisfies important game theoretic properties such as Bayesian incentive compatibility and individual rationality.

Aggregation of calcium ionophore (A23187) in phospholipid vesicles

The circular dichroism studies on calcium ionophore, A23187, incorporated in Dipalmitoyl phosphatidyl choline (DPPC) vesicle showed interesting time dependent changes in the CD spectra. Analysis of the data indicated the possible aggregation of the observed dimeric structure of this molecule in non-polar solvents into a stacked dimeric pore in the phospholipid vesicle.

X-ray studies on crystalline complexes involving amino acids and peptides. XV. Crystal structures of L-lysine D-glutamate and L-lysine D-aspartate monohydrate and the effect of chirality on molecular aggregation

L-Lysine D-glutamate crystallizes in the monoclinic space group P2(1) with a = 4.902, b = 30.719, c = 9.679 A, beta = 90 degrees and Z = 4. The crystals of L-lysine D-aspartate monohydrate belong to the orthorhombic space group P2(1)2(1)2(1) with a = 5.458, b = 7.152, c = 36.022 A and Z = 4. The structures were solved by the direct methods and refined to R values of 0.125 and 0.040 respectively for 1412 and 1503 observed reflections. The glutamate complex is highly pseudosymmetric. The lysine molecules in it assume a conformation with the side chain staggered between the alpha-amino and the alpha-carboxylate groups. The interactions of the side chain amino groups of lysine in the two complexes are such that they form infinite sequences containing alternating amino and carboxylate groups. The molecular aggregation in the glutamate complex is very similar to that observed in L-arginine D-aspartate and L-arginine D-glutamate trihydrate, with the formation of double layers consisting of both types of molecules. In contrast to the situation in the other three LD complexes, the unlike molecules in L-lysine D-aspartate monohydrate aggregate into alternating layers as in the case of most LL complexes. The arrangement of molecules in the lysine layer is nearly the same as in L-lysine L-aspartate, with head-to-tail sequences as the central feature. The arrangement of aspartate ions in the layers containing them is, however, somewhat unusual. Thus the comparison between the LL and the LD complexes analyzed so far indicates that the reversal of chirality of one of the components in a complex leads to profound changes in molecular aggregation, but these changes could be of more than one type.

Weak consistency of read-only transactions: A tool to improve concurrency in heterogeneous locking protocols

Three different types of consistencies, viz., semiweak, weak, and strong, of a read-only transaction in a schedule s of a set T of transactions are defined and these are compared with the existing notions of consistencies of a read-only transaction in a schedule. We present a technique that enables a user to control the consistency of a read-only transaction in heterogeneous locking protocols. Since the weak consistency of a read-only transaction improves concurrency in heterogeneous locking protocols, the users can help to improve concurrency in heterogeneous locking protocols by supplying the consistency requirements of read-only transactions. A heterogeneous locking protocol P' derived from a locking protocol P that uses exclusive mode locks only and ensures serializability need not be deadlock-free. We present a sufficient condition that ensures the deadlock-freeness of Pprime, when P is deadlock-free and all the read-only transactions in Pprime are two phase.

Effect of amino acid substitutions at the subunit interface on the stabiity and aggregation properties of a dimeric protein: role of Arg 178 and Arg 218 at the dimer interface of thymidylate synthase

The significance of two interface arginine residues on the structural integrity of an obligatory dimeric enzyme thymidylate synthase (TS) from Lactobacillus casei was investigated by thermal and chemical denaturation. While the R178F mutant showed apparent stability to thermal denaturation by its decreased tendency to aggregate, the Tm of the R218K mutant was lowered by 5 degrees C. Equilibrium denaturation studies in guanidinium chloride (GdmCl) and urea indicate that in both the mutants, replacement of Arg residues results in more labile quaternary and tertiary interactions. Circular dichroism studies in aqueous buffer suggest that the protein interior in R218K may be less well-packed as compared to the wild type protein. The results emphasize that quaternary interactions may influence the stability of the tertiary fold of TS. The amino acid replacements also lead to notable alteration in the ability of the unfolding intermediate of TS to aggregate. The aggregated state of partially unfolded intermediate in the R178F mutant is stable over a narrower range of denaturant concentrations. In contrast, there is an exaggerated tendency on the part of R218K to aggregate in intermediate concentrations of the denaturant. The 3 A crystal structure of the R178F mutant reveals no major structural change as a consequence of amino acid substitution. The results may be rationalized in terms of mutational effects on both the folded and unfolded state of the protein. Site specific amino acid substitutions are useful in identifying specific regions of TS involved in association of non-native protein structures.

CD and NMR studies on the aggregation of amphotericin-B in solution

We report in this paper the aggregation properties of amphotericin-B (amp-B) in solution using CD and 1H-NMR techniques. Our results indicate that the preferred structure of amp-B in dimethylsulfoxide is a monomer at low concentrations (10−4M and below) and a stable dimer at higher concentrations (range 5 · 103 M to 10−2M). In a DMSO/ethanol mixture (1:1 (v/v)), the antibiotic is monomeric, irrespective of the concentration within the range studied. We propose a head-to-tail model based on NMR data. An understanding of the head-to-tail dimer, is, we believe important, particularly in view of the recent report wherein it is proposed that the drug inserts into bilayers as head-to-tail oligomers.

Lipid-amphotericin B complex structure in solution: A possible first step in the aggregation process in cell membranes

The interactions between the polyene antibiotic amphotericin B with dipalmitoylphosphatidylcholine were investigated in vesicles (using circular dichroism) and in chloroform solution (using circular dichroism and IH, I3C, and 31P nuclear magnetic resonance). The results show that amphotericin B readily aggregates in vesicles and that the extent of aggregation depends on the 1ipid:drug concentration ratio. Introduction of sterol molecules into the membrane hastens the process of aggregation of amphotericin B. In chloroform solutions amphotericin B strongly interacts with phospholipid molecules to form a stoichiometric complex. The results suggest that there are interactions between the conjugated heptene stretch of amphotericin B and the methylene groups of lipid acyl chains, while the sugar moiety interacts with the phosphate head group by the formation of a hydrogen bond. A model is proposed for the lipid-amphotericin B complex, in which amphotericin B interacts equally well with the two lipid acyl chains, forming a 1:l complex.

Coordination aggregation of mesoaryl substituted porphyrins

Synthesis of the free-base tetrakis (3'-nitro/aminophenyl), (H2TNP/H(2)TAP) has been accomplished and its coordination behaviour towards Mg(II), Co(II), Zn(II) and Ag(II) ions is investigated. Optical and magnetic resonance properties of the metal derivatives MTNP and MTAP reveal that the aminoporphyrins exist as aggregates in solution. The aggregation is promoted by the coordination of the peripheral amino groups to neighbouring metalloporphyrins. Possible structures of aggregated species are proposed from the model studies.