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L Zetta

Publications and source records attributed to L Zetta.

51 records · Page 3Linked to original sources
PubMed1988

Reaction of 2-amino-2-deoxy-D-glucose and lysine: isolation and characterization of 2,5-bis(tetrahydroxybutyl)pyrazine.

The reaction of 2-amino-2-deoxy-D-glucose with lysine in water under simulated physiological conditions gave several browning products, with characteristic optical (lambda max 340 nm) and fluorescent properties (emission at 430 nm for excitation at 362 nm). The major product was isolated and characterized by mass spectrometry and n.m.r. spectroscopy as 2,5-bis(tetrahydroxybutyl)pyrazine derived by the condensation of two molecules of 2-amino-2-deoxy-D-glucose.

Chemical Phenomena↗
PubMed1986

Kringle 4 from human plasminogen: a proton magnetic resonance study via two-dimensional photochemically induced dynamic nuclear polarization spectroscopy.

Two-dimensional (2D) proton magnetic resonance techniques used in conjunction with laser photochemically induced dynamic nuclear polarization (photo-CIDNP) spectroscopy have been applied to studying the kringle 4 domain from human plasminogen at 360 MHz. Out of 11 potential CIDNP-sensitive aromatic side chains, only 5 (His3, Tyr41, Tyr50, Trp72, and Tyr74) appear to be accessible to 3-(carboxymethyl)lumiflavin, the dye used to photogenerate spin polarization. Of these, Trp72 and Tyr74 are known to be at, or near, the lysine-binding site. The spin-spin scalar (J) and phase-sensitive dipolar (Overhauser) connectivities in the 2D experiments yield absolute assignments for the aromatic signals stemming from the exposed tyrosyl and tryptophanyl rings. Moreover, a number of side-chain H beta resonances can be identified and assigned to specific types of aromatic amino acid residues.

Amino Acid Sequence↗
PubMed1986

1H-NMR of reverse micelles. II: Conformational studies of peptides and proteins in the AOT/water/isooctane system.

The interaction of AOT reverse micelles with Met-enkephalin, the pancreatic secretory trypsin inhibitor (PSTI) and the epidermal growth factor (EGF) is examined by NMR methods and the three systems are compared. While Met-enkephalin adopts a folded conformation, PSTI appears to become highly flexible, suggestive of a non-specific interaction with the micelles. On the other hand, the EGF spectrum shows that, although the main globular features of the protein are retained in the presence of AOT, the C-terminal fragment has to rearrange its conformation when put in contact with the micelle wall.

Dioctyl Sulfosuccinic Acid↗
PubMed1984

Interaction of beta-endorphin with sodium dodecyl sulfate in aqueous solution. 1H-NMR investigation.

1H-NMR spectra at 600 MHz and 270 MHz and photo-chemically induced dynamic nuclear polarization (photo-CIDNP) spectra at 360 MHz of beta-endorphin in the presence of sodium dodecyl sulfate (SDS) micelles are reported and discussed in terms of structural changes and immobilization upon binding. On addition of micelles several NH protons show slow H-D exchange rate in 2H2O at p2H 4.6, 25 degrees C, which indicates that some regions of the polypeptide are buried and shielded from the direct interaction with the solvent. Moreover, in the methyl region of the spectrum strong changes are detected both in chemical shifts and line-widths, suggesting an appreciable interaction between the hydrophobic residues of beta-endorphin and the detergent micelles. All aromatic residues are strongly affected by the presence of SDS, supporting the notion that beta-endorphin can interact with both the hydrophobic and hydrophilic portion of the micelles. At physiological pH photo-CIDNP experiments indicate that SDS has about the same immobilizing effect on Tyr-1 and Tyr-27 as n-dodecylphosphorylcholine.

Animals↗
PubMed1983

Investigation by photochemically-induced dynamic nuclear polarization and nuclear Overhauser enhancement 1H-NMR of the interaction between beta-endorphin and phospholipid micelles.

The photochemically-induced dynamic nuclear polarization technique has been used to investigate the access of a photoexcited flavin dye to tyrosyl and histidyl residues in [Met]enkephalin and human and camel beta-endorphins, both alone and in the presence of n-dodecylphosphorylcholine micelles. The results indicate that the mode of binding of Tyr-1, but not of residue 27, is similar in the two endorphins and differs from that of Tyr-1 in [Met]enkephalin. In human beta-endorphin, accessibility and mobility of Tyr-27 are strongly reduced in the presence of lipid at physiological pH, whereas in camel beta-endorphin His-27 becomes immobilized only at high pH. Moreover, nuclear Overhauser enhancement experiments suggest a rigidifying influence of the peptide on the polar head groups of the micelles.

Amino Acid Sequence↗
PubMed1982

270-MHz 1H nuclear-magnetic-resonance study of met-enkephalin in solvent mixtures. Conformational transition from dimethylsulphoxide to water.

1H spectra at 270 MHz of zwitterionic Met-enkephalin pentapeptide (Tyr-Gly-Gly-Phe-Met) in (C2H3)2SO/water mixtures are reported and discussed in terms of solvent-induced conformational transitions. The analysis of the chemical shifts, line widths, coupling constants and rotamer populations around chi 1 and chi 2 suggests that the conformational properties of Met-enkephalin in the two solvents are quite different. In aqueous solution, the preferred structure, characterized by the absence of intramolecularly hydrogen-bonded NH groups and head-to-tail interactions, very likely is an equilibrium of unfolded conformations with approximately equal energy. In (C2H3)2SO, the preferred structure is folded, with the Met-5 NH intramolecularly bonded and the Gly-3 NH protected from the solvent, while the Gly-2 and Phe-4 amide protons are solvent exposed. A conformational transition of Met-enkephalin from the intramolecularly bonded to the unbonded one takes place at about 40 mol-% water in (C2H3)2SO, involving the Met-5 NH proton and the Tyr-Gly-Gly fragment. The Phe-4 and Met-5 phi angles do not change appreciably, which suggest that an inversion at the Gly-3 residue of the folded form, responsible for the conformational transition, does not affect the C-terminal moiety. At about 70 mol-% water in (C2H3)2SO a change in the solvent mixture properties affects the chi 1 rotamer populations and the ring dynamics of the aromatic side chains. The line broadening of the Tyr-1 delta and epsilon proton resonances indicates a specific interaction of the N-terminal ring with the solvent.

Dimethyl Sulfoxide↗
PubMed1982

Human beta-endorphin. 270-MHz 1H-nuclear-magnetic-resonance study of glycyl residues in aqueous solution.

1H spectra at 270 MHz of the beta h-endorphin glycyl residues in aqueous solution are reported. The chemical shifts, coupling constants and temperature coefficients are compared with those of the glycyl residues in Met-enkephalin and in a random coil model peptide. The local conformation of Tyr-Gly-Gly-Phe-segment observed in Met-enkephalin is maintained in beta h-endorphin.

Endorphins↗
PubMedDate not supplied

The design of a specific ligand of HIV gp120.

The crystal structure of CD4 suggested that the C/G38 and C/L44 replacements with the consequent cystine bridge formation are compatible with the native structure of that molecular moiety. As the NQGSF sequence, corresponding to the 39-43 fragment of human CD4 protein, was found to be involved in the HIV gp120 interaction, it has been synthesized in a cyclic form by adding two cysteine residues at the amino and carboxy termini. 1H-NMR studies show that the predominant solution conformation of cyclo-[CNQGSFC] is a type II beta-turn centred on the NQGS segment. Structural and dynamic properties of the peptide are also analysed in relation to the in vitro activity.

Amino Acid Sequence↗
PubMedDate not supplied

The solution structure of the immunodominant and cell receptor binding regions of foot-and-mouth disease virus serotype A, variant A.

Abstract: The solution structure of a 20 amino acid long peptide corresponding to the region 141-160 of the envelope protein Vp1 from foot-and-mouth disease virus (FMDV) serotype A, variant A, has been determined by a combination of NMR experiments and computer calculations. The peptide contains both the immunodominant epitope as well as the sequence (RGD) used by the virus to bind the cell receptor in the initial stages of infection. These two sites have been shown to partially overlap. One hundred and thirty-five NMR distance constraints were used to obtain a set of 11 structures by distance geometry, minimization and molecular dynamics simulations. These structures were divided into two homogeneous families based upon backbone superimposition. The first and most populated family was characterized by a backbone RMS of 1.5 +/- 0.4 A, the second by a backbone RMS of 0.8 +/- 0.2 A. The two families had similar structural features and differed mainly in the backbone angles of G149. In the larger of the two families these angles favoured the formation of a loop comprising residues 147 to 152 and stabilized by a H-bond between NH of D147 and the CO of A152. In the second family, where this bond was absent, the peptide adopted in this region the shape of an irregular helix. The C-terminal half of the peptide (152-159) was similar in both families and largely helical. Similar structural features were also found within the VRGDS sequence (144-148) which was assigned to a beta-turn type IV. The features of the two families of structures were found to be different from those of the recently published X-ray structure of the antigenic loop of a chemically modified form of FMDV. Proposals accounting for these differences are provided which take into account the dual activity of the 141-160 sequence (i.e. antibody binding and cell invasion through receptor binding).

Amino Acid Sequence↗
PubMedDate not supplied

The solution conformational features of two highly homologous antigenic peptides of foot-and-mouth disease virus serotype A, variant A and USA, correlate with their serological properties.

The solution structure of a peptide corresponding to the VP1 region 141-160 of foot-and-mouth disease virus (FMDV) serotype A variant USA has been studied by NMR and computer calculations and compared with the results from a study on a highly homologous peptide deriving from serotype A, variant A. The two peptides differ in their serological behavior and contain the immunodominant epitope of the virus which partly overlaps with its receptor binding region. Distance constraints, derived both from 2D and 3D homonuclear NMR and 2D-heteronuclear NMR experiments, were combined with DG calculations to yield 50 structures. After refinement through EM and restrained molecular dynamics simulations the selected structures shared several general features. In particular the 151-158 region was a helix in all cases while a large loop similar to that found in peptide A but comprising less residues and stabilized by an H-bond between the side chains of D147 and S150 was found in the majority of structures. A further loop, common to all structures, was identified around the RGD sequence (145-147). This was different from that found in the corresponding region of peptide A as were the conformations of the individual residues within the RGDX sequence. The different structural features shown by the two peptides were rationalized in terms of the S148 (peptide A) to F148 (peptide USA) mutation. The second mutation, that at position 153 (L in A, P in USA) did not appear to affect the structure of the peptide significantly although the different dimensions of the loop in the central region and the type of H-bond stabilizing it could be potentially ascribed to this second mutation. All criteria used pointed to different structural features for the two peptides consistent with their serological behaviour.

Amino Acid Sequence↗