The Chemistry of Tryptophan in Peptides and Proteins

Fontana, Angelo; Toniolo, Claudio

doi:10.1007/978-3-7091-3262-3_4

Cited by 16 publications

(18 citation statements)

References 381 publications

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“…(iii) The significant risk of epimerization, intrinsic to the segment condensation approach, should be reduced as much as possible by planning N‐terminal and central segments with the achiral Aib residue at their C‐terminus (30,31). (iv) The presence of a Trp residue in the sequence suggests to avoid an acidolytic removal of the protecting groups from the final peptide (32,33).…”

Section: Resultsmentioning

confidence: 99%

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Synthesis, Preferred Conformation, and Membrane Activity of Medium‐Length Peptaibiotics: Tylopeptin B

Gobbo¹,

Poloni

Zotti

et al. 2010

Chem Biol Drug Des

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The solid-phase synthesis and full chemical characterization of the medium-length (14-amino acid residues) peptaibol with antibiotic properties of tylopeptin B, originally extracted from the fruiting body of the mushroom Tylopilus neofelleus, are described. These data are accompanied by the results on the solution-phase synthesis via the segment condensation approach of a selected, side-chain protected, analog. A solution conformational analysis, performed by the combined use of FTIR absorption, circular dichroism, and 2D-NMR (the latter technique coupled to molecular dynamics calculations), favors the conclusion that the 3D-structure of tylopeptin B is largely helical with a preference for the a-or the 3 10 -helix type depending upon the nature of the solvent. Helix topology and (partial) amphiphilic character are responsible for the observed membrane-modifying properties of this peptaibiotic.

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Section: Resultsmentioning

confidence: 99%

“…(iv) The presence of a Trp residue in the sequence suggests to avoid an acidolytic removal of the protecting groups from the final peptide (32,33).…”

Section: Peptide Synthesismentioning

confidence: 99%

Synthesis, Preferred Conformation, and Membrane Activity of Medium‐Length Peptaibiotics: Tylopeptin B

Gobbo¹,

Poloni

Zotti

et al. 2010

Chem Biol Drug Des

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“…The drop is maximum with melittin dissolved in pH 7 phosphate buffer, where it is in the monomeric state and randomly coiled in its conformation. The curve is multiphasic in nature; this aspect of trp photolysis kinetics and mechanism has been studied by other workers (Fontana and Toniolo, 1976;Nakagawa et al, 1977Nakagawa et al, , 1985Inoue et af., 1982), and is not of primary concern to us here. We just note that under the conditions chosen, a reduction of 50% of the trp emission intensity occurs in about 60 min of irradiation.…”

Section: Melittinmentioning

confidence: 87%

THE CONFORMATIONAL STATUS OF A PROTEIN INFLUENCES THE AEROBIC PHOTOLYSIS OF ITS TRYPTOPHAN RESIDUES: MELITTIN, β‐ LACTOGLOBULIN and THE CRYSTALLINS

Rao

Balasubramanian

1990

Photochem & Photobiology

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We have studied the aerobic photolysis of the tryptophan residues of the proteins melittin and beta-lactoglobulin when the proteins are in ordered conformations and when they are in randomly coiled states. The results suggest that the conformational status of the protein is a factor that influences the photolysis of the constituent tryptophan residues. This point appears to be of relevance to the photo-oxidation of the tryptophan residues of the eye lens proteins crystallins.

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“…An absorption band at approximately 500 nm is typically ascribed to a charge transfer complex (31). It is well established that indole derivatives, such as the Trp residue, act as donors in such complexes.…”

Section: Solid‐state Studiesmentioning

confidence: 99%

On the orange color of Z‐Trp‐ONP_o*

Moretto

Formaggio

Crisma

et al. 2005

The Journal of Peptide Research

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Out of all nitrophenyl esters of N(alpha)-protected alpha-amino acids Z-Trp-ONP(o) is the only one which is deep orange colored in the crystalline state. Any change in N(alpha)-protection, nature of amino acid, spatial separation between Trp and the ester-group or position of the nitro-substitutent in the aromatic ring of the ester function results in a loss of this characteristic property. We solved the molecular and crystal structure of Z-l-Trp-ONP(o) by X-ray diffraction analysis and investigated its color changes and visible (vis) and infrared (IR) absorption spectra in the solid state as a function of the amino acid derivative/KBr (w/w) ratio in the pellets. This investigation was extended to toluene solutions of different Z-Trp-ONP(o) concentrations by use of vis absorption and proton magnetic resonance spectroscopic techniques. The onset of the orange color correlates closely with the appearance of a concentration-dependent absorption band near 500 nm and concentration-dependent shifts of the urethane and indole NH proton resonances. Our observations can be explained by the formation of an intermolecular charge transfer complex involving the Trp indole and the -ONP(o) nitrophenyl as the donor and the acceptor moieties, respectively.

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The Chemistry of Tryptophan in Peptides and Proteins

Cited by 16 publications

References 381 publications

Synthesis, Preferred Conformation, and Membrane Activity of Medium‐Length Peptaibiotics: Tylopeptin B

Synthesis, Preferred Conformation, and Membrane Activity of Medium‐Length Peptaibiotics: Tylopeptin B

THE CONFORMATIONAL STATUS OF A PROTEIN INFLUENCES THE AEROBIC PHOTOLYSIS OF ITS TRYPTOPHAN RESIDUES: MELITTIN, β‐ LACTOGLOBULIN and THE CRYSTALLINS

On the orange color of Z‐Trp‐ONP_o*

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The Chemistry of Tryptophan in Peptides and Proteins

Cited by 16 publications

References 381 publications

Synthesis, Preferred Conformation, and Membrane Activity of Medium‐Length Peptaibiotics: Tylopeptin B

Synthesis, Preferred Conformation, and Membrane Activity of Medium‐Length Peptaibiotics: Tylopeptin B

THE CONFORMATIONAL STATUS OF A PROTEIN INFLUENCES THE AEROBIC PHOTOLYSIS OF ITS TRYPTOPHAN RESIDUES: MELITTIN, β‐ LACTOGLOBULIN and THE CRYSTALLINS

On the orange color of Z‐Trp‐ONPo*

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On the orange color of Z‐Trp‐ONP_o*