Chain‐length dependence for secondary structure formation of homo‐oligopep tides fromε‐<i>tert.</i>‐butyloxycarbonyl‐L‐lysine with a lipophilic <i>C</i>‐terminal group

Toniolo, Claudio; Bonora, Gian Maria; Lüscher, Immanuel F.; Schneider, Conrad H.

doi:10.1111/j.1399-3011.1984.tb02691.x

Cited by 4 publications

(2 citation statements)

References 19 publications

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“…In dipeptides, the unordered, self-associated structure appears to predominate. In the highest oligomers there is no evidence for the absorption at about 1655 cm-' , indicative of a-helix formation (13)(14)(15)(16). The presence of the weak band at about 1690 cm-' (13,17) strongly supports the view that the 0-sheet formed is, at least in part, of the antiparallel type.…”

Section: Con Formational Analysismentioning

confidence: 96%

“…The presence of the weak band at about 1690 cm-' (13,17) strongly supports the view that the 0-sheet formed is, at least in part, of the antiparallel type. In the t-Boc protected peptides, however, this assignment is not unambiguous, due to overlapping of thisband to the absorption of the urethane C=O stretching mode (14- 16,18). The frequencies of the amide A and amide I bands exclude the occurrence of folded, intramolecularly H-bonded structures (1 9).…”

Section: Con Formational Analysismentioning

confidence: 99%

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Synthetic homo‐oligomethionine chemoattractants

Bismara

Bonora

Toniolo

et al. 1985

International Journal of Peptide and Protein Research

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Using solution methods, we have synthesized several series of L‐methionine homooligopeptides from the dipeptide to the hexapeptide with either a free α‐carboxyl function or different C‐blocking groups (methoxy, benzyloxy, benzy‐lamino) and with N‐blocking groups of either the amide type (formyl, pivaloyl) or the urethane type (tert.‐butyloxycarbonyl). Compounds were compared to determine the combined effect of main‐chain length and presence and nature of N‐ and C‐blocking groups on conformation‐activity relationship. Each peptide was tested for its ability to induce rabbit peritoneal polymorphonuclear leukocytes in the presence of cytochalasin B to secrete granule enzymes. In parallel, a conformational analysis was carried out in the solid state and in solution, using infrared absorption and circular dichroism. The biological and conformational data are discussed in relation to a recently proposed model of the chemotactic peptide receptor of rabbit neutrophils.

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Section: Con Formational Analysismentioning

confidence: 96%

Section: Con Formational Analysismentioning

confidence: 99%

Synthetic homo‐oligomethionine chemoattractants

Bismara

Bonora

Toniolo

et al. 1985

International Journal of Peptide and Protein Research

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Physical Data of Oligomers

Rothe

1999

The Wiley Database of Polymer Properties

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(Cholestanyloxycarbonyl)benzyl esters as peptide substituents: Conformational properties of fully protected oligo‐L‐lysines with C‐terminal (cholestanyloxycarbonyl)benzyl and benzyl ester moieties

Toniolo

Bonora

Moretto

et al. 1986

Helvetica Chimica Acta

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This study involves L-lysine oligo peptides, protected at the N-terminus by the Nps and at the &-amino functions by Boc groups. Two series were prepared from dimer to octamer, one containing the p-[(cholestan-3/3-yloxy)carbonyl]benzyl, the other one the benzyl ester group at the C-terminus. Conformational analyses were performed by IR absorption. The occurrence of the intermolecular [i-structure in the solid state and in CHzC1, solution was demonstrated for the highest oligomers. The relative stabilities of the self-associated species were determined by adding a variety of polar solvents to the CHzC12 solutions. The cholestanyl-containing peptides have a lower propensity to self-aggregate than the bcnzyl-ester analogues. Self-aggregation and decreasing solubility run in parallel. It was also directly shown that soluble urea derivatives may disrupt intermolecular H-bonds in CH2CIz, a point of practical interest, particularly in solid-phase peptide synthesis.Introduction. ~ C-Terminal protecting groups containing the cholestanol moiety are promising tools in the synthesis and conformational analysis of peptides, since they enhance peptide solubilities in organic solvents of low polarity [ 1-51. In previous work, p -([4-(cholestan-3~-yloxy)succinyloxy]methyl} benzyl ( = Chsucb (formerly Suco)) peptide esters were mainly used, but their preparation is rather cumbersome. Therefore, other carboxyl substituents containing cholestanol were proposed [6], inter afia the p-[(cholestan-3P-yloxy)carbonyl]benzyl ( = Chocb (formerly Beco)) ester group. In the present communication, we describe two complete series of [Lys( Boc)], peptides with n = 2 to 8, both carrying at the N-terminus the Nps protecting group. At the C-terminus,

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Chain‐length dependence for secondary structure formation of homo‐oligopep tides fromε‐tert.‐butyloxycarbonyl‐L‐lysine with a lipophilic C‐terminal group

Cited by 4 publications

References 19 publications

Synthetic homo‐oligomethionine chemoattractants

Synthetic homo‐oligomethionine chemoattractants

Physical Data of Oligomers

(Cholestanyloxycarbonyl)benzyl esters as peptide substituents: Conformational properties of fully protected oligo‐L‐lysines with C‐terminal (cholestanyloxycarbonyl)benzyl and benzyl ester moieties

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