Conformational studies on model peptides

Maser, F.; Bode, K.; Pillai, V. N. Rajasekharan; Mutter, Manfred

doi:10.1007/bfb0017104

Cited by 21 publications

(3 citation statements)

References 162 publications

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“…The effect on /3-sheet structures is less clear; it seems to depend on the TFE concentration as well as the sheet length. Studies with homooligopeptides, host guest peptides (Goodman et al, 1971;Maser et al, 1984;Mutter & Altmann, 1985), and fragments of angiotensin II (Greff et al, 1976b) have shown the existence of /3-sheet structures over wide concentration ranges of TFE up to pure TFE solutions. A prerequisite for this /3-sheet formation was that the peptide exceeded the critical chain length of 7-9 residues.…”

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confidence: 99%

Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide

Eyk²,

et al. 1992

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The structure of a synthetic peptide comprising the 28 amino-terminal residues of actin has been examined by 1H-NMR and CD spectroscopy. The peptide is largely unstructured and flexible in solution but becomes increasingly structured at higher trifluoroethanol (TFE) concentrations. As judged by CD with the use of two additional peptides (actin 1-20 and actin 18-28), TFE induces formation of up to 48% helical content within residues 1-20, while residues 21-28 exhibit no helical propensity. Similar results were obtained by using NMR-derived distance information in restrained molecular dynamics calculations. The calculated structure of actin 1-28 peptide in 80% TFE is well defined for the first 23 residues with a backbone root mean square deviation of 0.5 A. Two helices are formed from residues 4-13 and 16-20, and a beta-turn is formed from residues 13-16. The N-terminal residues 1-3 exhibit increased flexibility and a helix-like conformation while the C-terminal residues 21-28 show no regular secondary structure. These results are compared with the predicted secondary structure and the structure of the corresponding sequence in the crystal structure of actin [Kabsch et al. (1990) Nature 347, 37-44]. The significance of the TFE-induced peptide structure is discussed.

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confidence: 99%

Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide

Eyk²,

et al. 1992

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“…TFE has been characterized as a structure-enhancing cosolvent. TFE has been shown to stabilize a variety of structures in peptides including /3-sheet (Goodman et al, 1971;Mutter & Altmann, 1985;Maser et al, 1984), /3-tum (Cann et al, 1987;Greff et al, 1976;Siligardi et al, 1987;Blanco et al, 1994), and -helix (Nelson & Kallenbach, 1989;Lu et al, 1984;Lehrman et al, 1990;Segawa et al, 1991;Marion et al, 1988;Jiméniz et al, 1987;Reutimann et al, 1981). The dielectric constant of TFE is approximately one-third that of water, and it was proposed that the net effect of TFE would be to strengthen the interactions between charged groups (Llinás & Klein, 1975;Nelson & Kallenbach, 1986).…”

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confidence: 99%

Calcium-Induced Dimerization of Troponin C: Mode of Interaction and Use of Trifluoroethanol as a Denaturant of Quaternary Structure

Slupsky¹,

Kay²,

Reinach³

et al. 1995

Biochemistry

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Protein aggregation can be a problem, especially as a large number of proteins become available for structural studies at fairly high concentrations using solution techniques such as NMR spectroscopy. The muscle regulatory protein troponin C (TnC) undergoes a calcium-induced dimerization at neutral pH with a dissociation constant for the dimerization of 0.4 mM at 20 degrees C. The present study indicates that the mode of dimerization involves the N-domain of one monomer interacting with the N-domain of another monomer. Addition of the solvent trifluoroethanol (TFE) to a concentration of 15%, v/v, results in a 10-fold increase in the dimer dissociation constant of calcium-saturated TnC (4 mM at 20 degrees C), making TnC predominantly a monomer for spectroscopic studies. Further, TFE, at the concentrations used herein, acts to perturb the quaternary structure of TnC without adversely affecting the secondary or tertiary structure as evidenced by minimal changes to its CD spectra and 1H, 13C, and 15N NMR chemical shifts.

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“…Several biologically active peptidcs are in the C-terminal peptide amide form. The synthesis of C-terminal pcptide amides is important for structure-activity (Bodanszky and Shechan 1966;Takashima et al 1968;Schally et al 1971;River et al 1972) correlations and conformational studies (Maser et al 1984). In the conventional method of peptide synthesis, the C-terminal peptide amides are generally prepare~ by converting the N-protected C-terminal amino acid to the amide by treating with ammonia (Chambers and Carpenter 1955;Izeboud and Bcyerman 1978) and the stepwise incorporation of amino acid residues toward the amino end.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of substance P partial sequential peptides on a photolytically removable 4-aminomethyl-3-nitrobenzoylaminomethyl polystyrene support

Haridasan

Pillai

1991

Proc. Indian Acad. Sci. (Chem. Sci.)

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Sequential peptides corresponding to substance P (6-11) were synthesised on a photocleavable 4-aminomethyl-3-nitrobenzoylaminomethyl polystyrene resin. This photoremovable polymeric support, useful for the synthesis of C-terminal peptide amides, was prepared from 4-bromomethyl-3-nitrobenzoylaminomethyl polystyrene by treatment with potassium phthalimide followed by hydrazinolysis. Amino acid residues were incorporated onto this support following the standard solid-phase methodology of peptide synthesis. The protected peptide amides were cleaved from the resin by photolysis with light of wavelength 350nm. The resin was used for the synthesis of peptides including the partial sequence corresponding to substance P (9-11) which was further subjected to stepwise synthesis to prepare substance P (6-11) in an overall yield of 88~. This approach combines the advantages of the photochemical deprotection of the 4-aminomethyl-3-nitro carboxyl protecting group, the polymer-supported peptide synthesis and the polymer-analogous functionalisation procedure to obtain the C-terminal peptide amide under mild conditions.

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Conformational studies on model peptides

Cited by 21 publications

References 162 publications

Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide

Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide

Calcium-Induced Dimerization of Troponin C: Mode of Interaction and Use of Trifluoroethanol as a Denaturant of Quaternary Structure

Synthesis of substance P partial sequential peptides on a photolytically removable 4-aminomethyl-3-nitrobenzoylaminomethyl polystyrene support

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