Reversible screw sense inversion of the 310-helix in a dehydropeptide

Pieroni, Osvaldo; Fissi, Adriano; Pratesi, Claudio; Temussi, Pier Andrea; Ciardelli, Francesco

doi:10.1021/ja00016a098

Cited by 54 publications

(42 citation statements)

References 2 publications

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“…24,28,29,47,51,77,[79][80][81][82][83][84][85][86] These helical models are important to understand chiral interaction originating in termini of a biological helical backbone, as well as to estimate the significance of the terminal moiety in the determination of a one-handed helix sense. [5][6][7][8][9][10][11][12][13] From the viewpoint, the present sequence designed with N-terminal Gly and achiral -amino acids can be regarded as another model to approach the above issues in protein-mimicking backbones.…”

Section: Discussionmentioning

confidence: 99%

Chiral interaction in Gly‐capped N‐terminal motif of 3₁₀‐helix and domino‐type induction in helix sense

Ousaka¹,

Inai²,

Okabe³

2006

Biopolymers

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Chiral interaction of helical peptide with chiral molecule, and concomitant induction in its helix sense have been demonstrated in optically inactive nonapeptide (1) possessing Gly at its N-terminus: H-Gly-(Delta(Z)Phe-Aib)(4)-OCH(3) (1: Delta(Z)Phe = Z-dehydrophenylalanine; Aib = alpha-aminoisobutyric acid). Spectroscopic measurements [mainly nuclear magnetic resonance (NMR) and circular diochroism (CD)] as well as theoretical simulation have been carried out for that purpose. Peptide 1 in the 3(10)-helix tends to adopt preferentially a right-handed screw sense by chiral Boc-L-amino acid (Boc: t-butoxycarbonyl). Induction in the helix sense through the noncovalent chiral domino effect should be derived primarily from the complex supported by the three-point coordination on the N-terminal sequence. Thus the 3(10)-helical terminus consisting of only alpha-amino acid residues enables chiral recognition of the Boc-amino acid molecule, leading to modulation of the original chain asymmetry. Dynamics in the helix-sense induction also have been discussed on the basis of a low-temperature NMR study. Furthermore, the inversion of induced helix sense has been achieved through solvent effects.

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Section: Discussionmentioning

confidence: 99%

Chiral interaction in Gly‐capped N‐terminal motif of 3₁₀‐helix and domino‐type induction in helix sense

Ousaka¹,

Inai²,

Okabe³

2006

Biopolymers

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“…16 -18 Boc-L-Ala-L1Phe-Gly-L1Phe-L-Ala-0Me showed reversible screw sense inversion of 3 10 -helix, depending on solvent and temperature conditions. 5 • 13 Also, Boc-LAla-L1Phe-L1Phe-NMA (NMA, N-methyl amide) took an incipient 310-helix ofboth left-and right-handed screw senses in the solid. 12 Thus, L-residue seems to show the character of left-handed screw sense when it is relatively C-terminally introduced to achiral helical peptides.…”

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confidence: 99%

A Study of Chain-Length Effect on Helical Screw Sense in Peptides Having an N-Terminal L-Leu Residue

Inai

Ashitaka

Hirabayashi

1999

Polym J

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ABSTRACT:In order to clarify which helical screw sense is dominated depending on chain-length of peptides when an L-residue is introduced into the N-terminal position of achiral helical segments, we prepared three kinds of peptides I-III: Boc-L-Leu-(Aib-LlPhe).-Aib-OMe (n=2--4) 1-111 (Boc, t-butoxycarbonyl; Aib, iX-aminoisobutyric acid; LlPhe, Z-dehydrophenylalanine; OMe, methoxy). Here the segment -(Aib-LlPhe).-Aib-OMe was used for an achiral backbone composed of two "enantiomeric" (left-/right-handed) helices. Peptides I-III were found to form a 310-type helical conformation in chloroform, from the position of amide I band in FT-IR spectra and solvent accessibility of NH resonances in 1 H NMR measurement. CD spectra of peptides 1-111 showed exciton couplets around 280 nm with a positive peak at longer wavelengths in chloroform, acetonitrile, methanol, and tetrahydrofuran. The sign of exciton couplets indicates that the main-chains prefer a left-handed screw sense. Consequently, anN-terminal L-Leu residue induces a left-handed screw sense preferentially, irrespective of chain lengths for achiral helical segments (5-9 residues). This result could be supported by conformational energy calculation on acetyl-L-Leu-(Aib-L1Phe)4-Aib-0Me, in which a left-handed helical conformation was predominant. Also, in the lowest-energy left-handed helix, anN-terminal L-Leu residue takes an irregular conformation that deviates from a left-handed 310-/iX-helical region in conformational space of (¢, ljl).KEY WORDSMost of L-amino acid residues are well recognized to prefer a right-handed screw sense in helical segments of proteins or peptides. On the other hand, L-residue was rarely found to ind.uce a left-handed screw sense for several peptides containing achiral helicogenic residues, Z-dehydrophenylalanine (L1Phe) 1 -13 or cx-aminoisobutyric acid (Aib) 14 • 15 : b.Phe For example, a left-handed 3 10 -helix in solution was seen in Ac-L1Phe-Gly-L1Phe-L-Ala-0Me (Ac, acetyl; OMe, methoxy) 13 or Boc-L-Pro-Aib-L-Ala-Aib-L-Ala-OMe (Boc, t-butoxycarbonyl). 16 Left-handed 3 10 -helices have also been observed in the crystalline state for Aib pep tides containing an L-residue in the C-terminal position. 16 -18 Boc-L-Ala-L1Phe-Gly-L1Phe-L-Ala-0Me showed reversible screw sense inversion of 3 10 -helix, depending on solvent and temperature conditions. 5 • 13 Also, Boc-LAla-L1Phe-L1Phe-NMA (NMA, N-methyl amide) took an incipient 310-helix ofboth left-and right-handed screw senses in the solid. 12 Thus, L-residue seems to show the character of left-handed screw sense when it is relatively C-terminally introduced to achiral helical peptides.On the other hand, little is known about effect of N-terminal L-residue on dominating helical screw sense in achiral peptides. Recently, 19 we investigated this effect t To whom correspondence should be addressed. 246using Boc-X-(Aib-L1Phe)z-Aib-0Me, in which an Lamino acid residue (X) is introduced into the N-terminal position of achiral helical segment -(Aib-L1Phe)zAib-0Me composed of Aib and L1Phe res...

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“…The peptides contain a ∆Phe residue which gives a large CD band in that region, at about 280 nm, which is very sensitive to a dehydropeptide conformation. 18,19,[27][28][29][30][31][32][33][34][35][36][37][38][39][40][41][42][43][44] Thus, this residue is a very good conformational probe in the studies on dehydropeptides. Moreover, Z-p-NA and E-p-NA contain the p-NA group which has been also found to be a useful tool in the conformational studies on peptides.…”

Section: Discussionmentioning

confidence: 99%

Effect of the ΔPhe residue configuration on a didehydropeptides conformation: A combined CD and NMR study

Lisowski

Jaremko

et al. 2010

Biopolymers

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Conformations of two pairs of dehydropeptides with the opposite configuration of the ∆Phe residue, Boc-Gly-∆ Z Phe-Gly-Phe-OMe (Z-OMe), Boc-Gly-∆ E Phe-Gly-Phe-OMe (E-OMe), BocGly-∆ Z Phe-Gly-Phe-p-NA (Z-p-NA), and Boc-Gly-∆ E Phe-Gly-Phe-p-NA (E-p-NA) were compared on the basis of CD and NMR studies in MeOH, TFE, MeCN, chloroform, and DMSO. The CD results were used as the additional input data for the NMR-based determination of the detailed solution conformations of the peptides. It was found that E-OMe is unordered and Z-OMe, Z-p-NA, and E-p-NA adopt the β-turn conformation. There are two overlapping β-turns in each of those peptides: type II and type III' in Z-OMe and Z-p-NA, and two type III in E-p-NA. The ordered structure-inducing properties of ∆ Z Phe and ∆ E Phe in the peptides studied depend on the Cterminal blocking group. In methyl esters the ∆ Z Phe residue is a strong inducer of ordered conformations whereas the ∆ E Phe one has no such properties. In p-nitroanilides, both isomers of ∆Phe cause the peptides to adopt ordered structures to a similar extent.

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Reversible screw sense inversion of the 310-helix in a dehydropeptide

Cited by 54 publications

References 2 publications

Chiral interaction in Gly‐capped N‐terminal motif of 3₁₀‐helix and domino‐type induction in helix sense

Chiral interaction in Gly‐capped N‐terminal motif of 3₁₀‐helix and domino‐type induction in helix sense

A Study of Chain-Length Effect on Helical Screw Sense in Peptides Having an N-Terminal L-Leu Residue

Effect of the ΔPhe residue configuration on a didehydropeptides conformation: A combined CD and NMR study

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Reversible screw sense inversion of the 310-helix in a dehydropeptide

Cited by 54 publications

References 2 publications

Chiral interaction in Gly‐capped N‐terminal motif of 310‐helix and domino‐type induction in helix sense

Chiral interaction in Gly‐capped N‐terminal motif of 310‐helix and domino‐type induction in helix sense

A Study of Chain-Length Effect on Helical Screw Sense in Peptides Having an N-Terminal L-Leu Residue

Effect of the ΔPhe residue configuration on a didehydropeptides conformation: A combined CD and NMR study

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Chiral interaction in Gly‐capped N‐terminal motif of 3₁₀‐helix and domino‐type induction in helix sense

Chiral interaction in Gly‐capped N‐terminal motif of 3₁₀‐helix and domino‐type induction in helix sense