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402 results on '"Di Blasio, B."'

102. Non coded Cα,α‐disubstituted amino acids

Author

PAVONE, V., primary, DI BLASIO, B., additional, LOMBARDI, A., additional, MAGLIO, O., additional, ISERNIAI, C., additional, PEDONE, C., additional, BENEDETTI, E., additional, ALTMANN, E., additional, and MUTTER, M., additional

Published
1993
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125. Bioactive Peptides: Solid State and conformation of Cyclolinopeptide A

Author

Di Blasio B., Benedetti E., Pedone C., Temussi P. A, Zanotti G., Tancredi T., ROSSI, FILOMENA, PAVONE, VINCENZO, Di Blasio, B., Rossi, Filomena, Benedetti, E., Pavone, Vincenzo, Pedone, C., Temussi P., A, Zanotti, G., and Tancredi, T.

Subjects
cyclic peptide, NMR spectroscopy, isomerism of the Pro-Pro bound, isoenergetic conformation, X-ray crystal structure
Abstract

We reported the solid state and solution conformational analysis of Cyclolinopetide A, a cyclic nonapetide from linseed.

Published
1989

129. Conformation of linear homo‐oligo-prolines

Author

BENEDETTI E., BAVOSO A., DI BLASIO B., PEDONE C., TONIOLO C., BONORA G., PAVONE, VINCENZO, Benedetti, E., Bavoso, A., DI BLASIO, B., Pavone, Vincenzo, Pedone, C., Toniolo, C., and Bonora, G.

Published
1982

131. Food Proteins: Chemistry, Structure and Function of Wheat Bread-gliadins

Author

PAVONE, VINCENZO, ANDINI, SALVATORE, BENEDETTI, ETTORE, FERRARA, LUCIANO, PEDONE, CARLO, PUCCI, PIETRO, Di Blasio B., Pavone, Vincenzo, Andini, Salvatore, Benedetti, Ettore, Di Blasio, B., Ferrara, Luciano, Pedone, Carlo, and Pucci, Pietro

Subjects
function, wheat bread-gliadins, Food protein, structure
Published
1983

132. Modified calmodulin calcium binding domain III. Solid phase synthesis, purification and proton NMR characterization

Author

PAVONE, VINCENZO, ANDINI, SALVATORE, FERRARA, LUCIANO, BENEDETTI, ETTORE, PUCCI, PIETRO, Di Nola A., Di Blasio B., Pavone, Vincenzo, Di Nola, A., Andini, Salvatore, Ferrara, Luciano, Di Blasio, B., Benedetti, Ettore, and Pucci, Pietro

Subjects
Modified calmodulin, calcium binding domain III, NMR, purification, solid phase synthesi
Abstract

Dodecapeptide Ac-Asp-Lys-Asp-Gly-Asn-Gly-Tyr-Ile-Ser-Ala-Ala-Gaba-OH [I, Gaba = NH(CH2)3CO] was prepd. by the solid phase method with a total protection scheme using PAM-resin. Purified I was characterized by 1H NMR spectroscopy, both in the presence and in the absence of calcium ions at various pH values. No strong specific interaction occurred between I and Ca2+ in aq. solns.

Published
1984

135. Peptaibol antibiotics: a study on the helical structure of the 2-9 sequence of emerimicins III and IV.

Author

Benedetti, E, Bavoso, A, Di Blasio, B, Pavone, V, Pedone, C, Toniolo, C, and Bonora, G M

Abstract

Solution conformations of the protected 2-9 segment of the peptaibol antibiotics emerimicins III and IV [alpha-aminoisobutyric acid (Aib)]3-L-Val-Gly-L-Leu-(Aib)2 and the related short sequences benzyloxy-(Aib)3-L-Val-OMe and benzyloxy-(Aib)3-L-Val-Gly-OMe have been investigated by circular dichroism studies. For the latter two compounds the structural preferences in the solid state have been assayed by x-ray diffraction analyses. The experimental data described here, along with those previously reported, support the view that the shortest Aib-containing segments (from tri- through pentapeptides) adopt the 3(10)-helical structure both in solution and in the solid state. In contrast, the octapeptide appears to adopt the alpha-helical structure in solution. The role of peptide chain length and specific amino acid sequences in stabilizing either of the two helical structures and hence their possible implications on the nature of the channel formed by peptaibol antibiotics in the membrane are also briefly outlined.

Published
1982
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136. Structure of N-acetyl-D-alanyl-D-alanine hydrate. An analogue of the COOH-terminal segment of peptidoglycan of bacterial cell walls.

Author

Benedetti, E, Di Blasio, B, Pavone, V, Pedone, C, Toniolo, C, and Bonora, G M

Abstract

The solid state conformational analysis of Ac-D-Ala-D-Ala-OH.H2O, carried out by infrared absorption and X-ray diffraction, has indicated that the molecules are not extended in a regular beta conformation, but rather that they are partially folded, the phi, psi torsional angles of the COOH-terminal residue in particular being in the region of the left-handed alpha helix of the Ramachandran map. The acetylamino and peptide groups ar found in the usual trans conformation, the latter, however, exhibiting a deviation from rigid planarity. Only intermolecular hydrogen bonds occur in the crystal state. The solution conformational analysis, performed by infrared absorption and CD, has revealed that the amount of intramolecular N--H ... O==C hydrogen-bonded folded forms, if any, should be extremely small, even in deuteriochloroform at high dilution. In water, solvated, unordered species largely predominate.

Published
1981
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137. Structure of N-tert-butyloxycarbonyl-D-leucyl-L-phenylalanylethanolamide. An N alpha-protected analogue of the COOH-terminal dipeptide of linear gramicidins.

Author

Bonora, G M, Toniolo, C, Bavoso, A, Benedetti, E, Di Blasio, B, Pavone, V, and Pedone, C

Abstract

Solid state conformational analysis of N-tert-butyloxycarbonyl-D-leucyl-L-phenylalanylethanolamide (t-Boc-D-Leu-L-Phe-EA), an N alpha-protected analogue of the COOH-terminal dipeptide of linear gramicidins, carried out by x-ray diffraction, has indicated that the molecules are characterized by an N-H..O = C intramolecularly hydrogen-bonded chain reversal of the beta-turn II' type. One of the two independent molecules in the asymmetric unit shows an additional intramolecular hydrogen bond of the O-H..O = C type, linking the hydroxyl function of the COOH-terminal ethanolamide moiety to the carbonyl oxygen of the urethane N-protecting group. This is the first experimental evidence for a beta-turn conformation fused with the oxy analogue of an alpha-turn. The results of an investigation in a solvent of low polarity (deuteriochloroform), using infrared absorption and 1' nuclear magnetic resonance, strongly support the view that an intramolecularly hydrogen-bonded beta-turn conformation is the most populated conformation of t-Boc-D-Leu-L-Phe-EA molecules at high dilution. In the self-association process, taking place at high concentration, the urethane and peptide NH groups are involved as hydrogen-bonding donors.

Published
1983
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139. CONFORMATIONAL ANALYSIS OF N-TERT AMYLOXYCARBONYL-L PROLINE IN THE SOLID STATE AND IN SOLUTION

Author

BENEDETTI E, CIAJOLO A, DI BLASIO B, PAVONE V, PEDONE C, TONIOLO C, and BONORA G M

Subjects
peptitid, diffrattometria
Abstract

Solid-state conformational analysis of N-tert-amyloxycarbonyl-L-proline indicated that the molecules are not folded up to form an oxy-C7 peptide conformation, but are held together through intermolecular O-H .... O .dbd. C (urethane) H-bonds. The tertiary amide bond is in the cis configuration. In solvents of high polarity strongly solvated species largely predominate. In cyclohexane solution non-associated and associated (involving the carboxyl C .dbd. O as the proton acceptor) species are simultaneously present. The extent of association increases with increasing solute concentration. The amount of the oxy-C7 form, if any, should be extremely small. It is also demonstrated that circular dichroism measurements alone can lead to an incorrect picture of the conformational preferences of amino acid derivatives and small peptides in solution.

Published
1979

150. Preferred conformation of peptides rich in Ac8c, a medium-ring alicyclic Cα,α-disubstituted glycine

Author

Michele Saviano, Antonello Santini, Moretto, Di Blasio B, Claudio Toniolo, Carlo Pedone, Fernando Formaggio, Gian Maria Bonora, Marco Crisma, and Ettore Benedetti

Subjects
Models, Molecular, Magnetic Resonance Spectroscopy, Protein Conformation, Pentamer, Stereochemistry, Glycine, Amino Acids, Cyclic, Tripeptide, Biochemistry, chemistry.chemical_compound, Alicyclic compound, Residue (chemistry), Protein structure, X-Ray Diffraction, Structural Biology, Spectroscopy, Fourier Transform Infrared, Drug Discovery, Amino Acids, Molecular Biology, gamma-Aminobutyric Acid, Pharmacology, chemistry.chemical_classification, Dipeptide, Organic Chemistry, General Medicine, Amino acid, chemistry, Helix, Molecular Medicine, Peptides
Abstract

A complete series of terminally blocked, monodispersed homo-oligopeptides (to the pentamer level) from the sterically demanding, medium-ring alicyclic C (alpha,alpha)-disubstituted glycine 1-aminocyclooctane-1-carboxylic acid (Ac8c), and two Ala/Ac8c tripeptides, were synthesized by solution methods and fully characterized. The preferred conformation of all the oligopeptides was determined in deuterochloroform solution by IR absorption and 1H-NMR. The molecular structures of the amino acid derivative Z-Ac8c-OH, the dipeptide pBrBz-(Ac8c)2-OH and the tripeptide pBrBz-(Ac8c)3-OtBu were assessed in the crystal state by X-ray diffraction. Conformational energy computations were performed on the monopeptide Ac-Ac8c-NHMe. Taken together, the results obtained strongly support the view that the Ac8c residue is an effective beta-turn and helix former. A comparison is also made with the conformational preferences of alpha-aminoisobutyric acid, the prototype of C (alpha,alpha)-disubstituted glycines, and of the other members of the family of 1-aminocycloalkane-1-carboxylic acids (Acnc with n = 3, 5-7) investigated so far. The implications for the use of the Ac8c residue in peptide conformational design are considered.

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