The size of electron-hole pairs in pi conjugated systems

We have performed momentum dependent electron energy-loss studies of the electronic excitations in sexithiophene and compared the results to those from parent oligomers. Our experiment probes the dynamic structure factor S(q,omega)and we show that the momentum dependent intensity variation of the excitations observed can be used to extract the size of the electron-hole pair created in the excitation process. The extension of the electron-hole pairs along the molecules is comparable to the length of the molecules and thus maybe only limited by structural constraints. Consequently, the primary intramolecular electron-hole pairs are relatively weakly bound. We find no evidence for the formation of excitations localized on single thiophene units.Comment: RevTex, 3 figures, to appear in Physical Review Letter

Low pH enhances the action of maximin H5 against Staphylococcus aureus and helps mediate lysylated phosphatidylglycerol induced resistance

Maximin H5 (MH5) is an amphibian antimicrobial peptide specifically targeting Staphylococcus aureus. At pH 6, the peptide showed an increased ability to penetrate (∆П = 6.2 mN m-1) and lyse (lysis = 48 %) S. aureus membrane mimics, which incorporated physiological levels of lysylated phosphatidylglycerol (Lys-PG, 60 %) as compared to pH 7 (∆П = 5.6 mN m-1 and lysis = 40 % at pH 7) where levels of Lys-PG are lower (40 %). The peptide therefore appears to have optimal function at pH levels known to be optimal for the organism’s growth. MH5 killed S. aureus (minimum inhibitory concentration = 90 µM) via membranolytic mechanisms that involved the stabilization of α-helical structure (circa 45-50 %) and which showed similarities to the ‘Carpet’ mechanism based on its ability to increase the rigidity (Cs-1 = 109.94 mN m-1) and thermodynamic stability (∆Gmix = -3.0) of physiologically relevant S. aureus membrane mimics at pH 6. Based on theoretical analysis this mechanism may involve the use of a tilted peptide structure and efficacy was noted to vary inversely with the Lys-PG content of S. aureus membrane mimics for each pH studied (R2 circa 0.97), which led to the suggestion that under biologically relevant conditions, low pH helps mediate Lys-PG induced resistance in S. aureus to MH5 antibacterial action. The peptide showed a lack of haemolytic activity (< 2 % haemolysis) and merits further investigation as a potential template for development as an anti-staphylococcal agent in medically and biotechnically relevant areas

Linear and nonlinear optical properties of the conjugated polymers PPV and MEH-PPV

We have used absorption and electroabsorption spectroscopy to investigate the electronic structure of poly(para-phenylene vinylene) (PPV) and poly (2-methoxy, 5-(2'-(ethyl)hexyloxy)-p-phenylene vinylene) (MEH-PPV). In particular we examine the often used assumption that the electronic structure of PPV and its dialkoxy substituted derivatives are essentially the same. The absorption spectrum of PPV consists of three peaks, while that of MEH-PPV has four peaks. We discuss the controversial origin of the extra peak as well as evidence for Davydov splitting effects in the absorption spectrum of PPV. The analysis of the nonlinear spectra shows further differences between the two materials. First, the binding energy of the 1B(u) exciton for PPV is some 0.1 eV higher than for MEH-PPV. Second, the peak value of Im{chi((3))(-omega;0,0,omega)} for PPV is approximately 40 times higher than that of MEH-PPV. We also found that the sum-over-states modeling of the electroabsorption spectra indicates that the transition dipole moment between the mA(g) and nB(u) states is of opposite sign in the two polymers. [S0163-1829(99)02523-0]