OFF-ON-OFF fluorescent response of N,N,N',N'-tetrakis(1-isoquinolylmethyl)-2-hydroxy-1,3-propanediamine (1-isoHTQHPN) toward Zn(2.).

An isoquinoline-based ligand, N,N,N',N'-tetrakis(1-isoquinolylmethyl)-2-hydroxy-1,3-propanediamine (1-isoHTQHPN), exhibits a fluorescence increase at 475 nm upon addition of 1 equiv. of Zn(2+) (IZn/I0 = 12, ϕZn = 0.023). This fluorescence enhancement turns and then decreases sharply after the addition of more than 1 equiv. of Zn(2+) reaching a constant minimum intensity with more than 2 equiv. of Zn(2+). In contrast, the fluorescence intensity at 353 nm continues to increase until the signal saturates at ca. 5 equiv. of Zn(2+). This observation can be explained by the formation of a fluorescent mononuclear complex ([Zn(1-isoHTQHPN)](2+)) followed by a non-fluorescent dinuclear complex ([Zn2(1-isoTQHPN)](3+)) at 475 nm during the titration of 1-isoHTQHPN with Zn(2+). Both the mono- and dinuclear complexes were characterized by UV-vis, fluorescence, (1)H NMR, ESI-MS, X-ray crystallography and TDDFT calculations. The fluorescence enhancement at 475 nm is Zn(2+)-specific; Cd(2+) induces a much smaller emission increase (ICd/I0 = 3.7, ICd/IZn = 31%). The Zn(2+)/Cd(2+) selectivity of the fluorescent response correlates with the difference in excimer-forming ability derived from the Cd-Nisoquinoline and Zn-Nisoquinoline bond distances.

Effects of pyrenebutyrate on the translocation of arginine-rich cell-penetrating peptides through artificial membranes: recruiting peptides to the membranes, dissipating liquid-ordered phases, and inducing curvature.

Arginine-rich cell-penetrating peptides, including octaarginine (R8) and HIV-1 TAT peptides, have the ability to translocate through cell membranes and transport exogenous bioactive molecules into cells. Hydrophobic counteranions such as pyrenebutyrate (PyB) have been reported to markedly promote the membrane translocation of these peptides. In this study, using model membranes having liquid-ordered (Lo) and liquid-disordered (Ld) phases, we explored the effects of PyB on the promotion of R8 translocation. Confocal microscopic observations of giant unilamellar vesicles (GUVs) showed that PyB significantly accelerated the accumulation of R8 on membranes containing negatively charged lipids, leading to the internalization of R8 without collapse of the GUV structures. PyB displayed an alternative activity, increasing the fluidity of the negatively charged membranes, which diminished the distinct Lo/Ld phase separation on GUVs. This was supported by the decrease in fluorescence anisotropy of 1,6-diphenyl-1,3,5-hexatriene (DPH). Additionally, PyB induced membrane curvature, which has been suggested as a possible mechanism of membrane translocation for R8. Taken together, our results indicate that PyB may have multiple effects that promote R8 translocation through cell membranes.

Translational diffusion coefficient of cycloamylose in aqueous sodium hydroxide.

Seven cyclic (1 --> 4)-alpha-D-glucan (cycloamylose) samples ranging in weight-average molecular weight from 5 x 10(3) to 1.8 x 10(4) and gamma-cyclodextrin have been studied by sedimentation equilibrium in dimethylsulfoxide (at 25 degrees C) and by dynamic light scattering in 0.5 N aqueous sodium hydroxide (at 25 degrees C), a good solvent for linear amylose. The measured translational diffusion coefficients D in the aqueous NaOH agree fairly closely with previous Monte Carlo results for cyclic (1 --> 4)-alpha-D-glucan chains with excluded volume, when correction is made for the effects of bead diameter and fluctuating hydrodynamic interaction (HI) on the Kirkwood theory on which the computation of D was based. These D data are also explained almost quantitatively by Yamakawa and Fujii's expression for the associated KP ring (based on the Kratky-Porod wormlike chain) with the molecular parameters for linear amylose if the fluctuating HI and excluded-volume effects are taken into account. It is concluded that the translational diffusion behavior of cycloamylose in the aqueous NaOH is consistent with the conformational characteristics derived from the conformational energy of maltose and dilute-solution data for linear amylose.

Monte Carlo study of cycloamylose: chain conformation, radius of gyration, and diffusion coefficient.

Cyclic (1 --> 4)-alpha-D-glucan chains with or without excluded volume have been collected from a huge number (about 10(7)) of linear amylosic chains generated by the Monte Carlo method with a conformational energy map for maltose, and their mean-square radii of gyration and translational diffusion coefficients D (based on the Kirkwood formula) have been computed as functions of x (the number of glucose residues in a range from 7 to 300) and the excluded-volume strength represented by the effective hard-core radius. Both /x and D in the unperturbed state weakly oscillate for x < 30 and the helical nature of amylose appears more pronouncedly in cyclic chains than in linear chains. As x increases, these properties approach the values expected for Gaussian rings. Though excluded-volume effects on them are always larger in cycloamylose than in the corresponding linear amylose, the ratios of and the hydrodynamic radius of the former to the respective properties of the latter in good solvents can be slightly lower than or comparable to the (asymptotic) Gaussian-chain values when x is not sufficiently large. An interpolation expression is constructed for the relation between the gyration-radius expansion factors for linear and cyclic chains from the present Monte Carlo data and the early proposed asymptotic relation with the aid of the first-order perturbation theories.