1995
DOI: 10.1021/bi00008a022 View full text |Buy / Rent full text
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Abstract: 1D and 2D NMR spectroscopy is used to determine the helical stability of two Aib-rich peptides, iBoc-(Aib)3-DkNap-Leu-Aib-Ala-(Aib)2-NH(CH2)2OCH3 (Dk4[7/9]) and Ac-(Aib)2-beta-(1'-naphthyl)Ala-(Aib)2-Phe-(Aib)2-NHMe (Nap3Phe6[6/8]), where the bracket notation indicates the number of Aib-class residues/total number of residues. 2D ROESY experiments, carried out previously on Nap3Phe6[6/8] in DMSO (Basu & Kuki, 1993), showed that this compound adopts the 3(10)-helical conformation at 20 degrees C. The first step… Show more

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“…The most thermal-sensitive residue, Glyl 1, exhibits a linear shift of only -7 ppb/"C. The small ( + I to +3 ppb/"C), linear thermal dependence of the N-acetyl carbonyl and the carbonyls of Ala(Me) residues I , 3, 5 , and 13 suggest that, over the 80°C temperature range studied, these residues are the most conformationally stable in the peptide. As most of these residues occur in the N-terminus, this interpretation is in agreement with the data which suggests that the N-terminus of alamethicin is more stable than the C-terminus (Esposito et al, 1987;Yee and O'Neil, 1992;Franklin et al, 1994;Yee et al, 1995) and that Ala(Me) residues can give remarkable conformational stability to helical peptides (Augspurger et al, 1995). The presence of an N-acetyl group may add additional stability to the N-terminus of the helix (Chakrabartty et al, 1993;Jung et al, 1983).…”
Section: Temperature Dependence Of the Carbonyl Chemical Shiftssupporting
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rupbmjkragerfmgwileyiopcupepmcmbcthiemesagefrontiersapsiucrarxivemeralduhksmucshluniversity-of-gavle
“…The most thermal-sensitive residue, Glyl 1, exhibits a linear shift of only -7 ppb/"C. The small ( + I to +3 ppb/"C), linear thermal dependence of the N-acetyl carbonyl and the carbonyls of Ala(Me) residues I , 3, 5 , and 13 suggest that, over the 80°C temperature range studied, these residues are the most conformationally stable in the peptide. As most of these residues occur in the N-terminus, this interpretation is in agreement with the data which suggests that the N-terminus of alamethicin is more stable than the C-terminus (Esposito et al, 1987;Yee and O'Neil, 1992;Franklin et al, 1994;Yee et al, 1995) and that Ala(Me) residues can give remarkable conformational stability to helical peptides (Augspurger et al, 1995). The presence of an N-acetyl group may add additional stability to the N-terminus of the helix (Chakrabartty et al, 1993;Jung et al, 1983).…”
Section: Temperature Dependence Of the Carbonyl Chemical Shiftssupporting
“…The sensitivity of their carbonyls to Me,SO suggests that intramolecular hydrogen bonding is comparatively weak in those regions of the peptide. The results of Augspurger et al (1995) indicate that an Ala(Me)-rich (77 %) nonapeptide is 3," helical and thermally stable up to 150°C in both chloroform and Me,SO. The thermal behaviour of alamethicin 140% Ala(Me)] in methanol is intermediate between the cooperative unfolding of alanine-based peptides in water and the thermal insensitivity of high-Ala(Me) peptides dissolved in non-polar solvents.…”
Section: Temperature Dependence Of the Carbonyl Chemical Shiftsmentioning
“…The Aib residue confers remarkable thermal stability to host peptides, increasing the melting temperature of a reengineered protein, 36 and conferring helix melting temperatures exceeding the boiling point of NMR solvents (e.g., in excess of 55°C for a homodecamer of Aib in CDCl 3 , 37 and in excess of 150°C for an octamer containing six Aib residues 38 ). Recently, the melting temperature of a 14-residue sequence including Aib was found to be the same as an alaninebased analogue of 26 residues.…”
Section: Introductionmentioning
“…Our long-standing experience on medium-sized 3 10 -helical peptides based entirely on the strongly helicogenic C a -tetrasubstituted a-amino acid Aib, [5d,e] along with literature data on a variety of peptides from this series from other research groups, [11] make us quite confident that the overwhelmingly preferred conformation (3 10 -helix) of the -CO-(Aib) 6 -O-sequence used in this study is extremely resistant to melting, particularly under the rela- tively mild experimental conditions (heating to 50-55 8C in solvents of low polarity, such as CHCl 3 or CH 3 CN) required for activating our peptido [2]rotaxane molecular machine. Our results also suggest that changing the solvent from CHCl 3 to CH 3 CN results in modification of the relative stabilities of the two stations (Z)-MAL diamide and -d-Leu-Gly-Gly-in IVa and IV b, respectively.…”
Section: Methodsmentioning