Conformational behavior of Cα,α-diphenyl glycine: Extended conformation in tripeptides containing consecutive Dφg residues

Pavone, Vincenzo; Lombardi, Angela; Simone, Giuseppina De; Nastri, Flavia; Maglio, Ornella; Omote, Yuichiro; Yamanaka, Yoshinori; Yamada, Takashi

doi:10.1002/(sici)1097-0282(2000)53:2<161::aid-bip6>3.3.co;2-z

Cited by 6 publications

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“…The preferred conformation of the C α,α ‐symmetrically disubstituted glycines DΦg ( C α,α ‐diphenyglycine), Db z g ( C α,α ‐dibenzylglycine), and Dtg ( C α,α ‐dimethylthioethylglycine) (Figure 1) were also examined and found to be similar to those of the Aib higher homologs discussed above 66–70. Interestingly, in the Dp

_{2}^{y}

g [C α,α ‐di(2‐pyridyl)glycine] (Figure 1) peptides in solution the extended structure seems to be stabilized by two (side‐chain) N … HN (main‐chain) intramolecular H‐bonds per Dp

_{2}^{y}

g unit, forming C 6 pseudocyclic systems 68…”

Section: Discussionmentioning

confidence: 87%

Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)

et al. 2001

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The preferred conformations of peptides heavily based on the currently extensively exploited achiral and chiral α‐amino acids with a quaternary α‐carbon atom, as determined by conformational energy computations, crystal‐state (x‐ray diffraction) analyses, and solution (1H‐NMR and spectroscopic) investigations, are reviewed. It is concluded that 310/α‐helical structures and the fully extended (C5) conformation are preferentially adopted by peptide sequences characterized by this family of amino acids, depending upon overall bulkiness and nature (e.g., whether acyclic or C αi ↔ C αitalici cyclized) of their side chains. The intriguing relationship between α‐carbon chirality and bend/helix handedness is also illustrated. γ‐Bends and semiextended conformations are rarely observed. Formation of β‐sheet structures is prevented. © 2002 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 60: 396–419, 2001

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_{2}^{y}

g [C α,α ‐di(2‐pyridyl)glycine] (Figure 1) peptides in solution the extended structure seems to be stabilized by two (side‐chain) N … HN (main‐chain) intramolecular H‐bonds per Dp

_{2}^{y}

g unit, forming C 6 pseudocyclic systems 68…”

Section: Discussionmentioning

confidence: 87%

Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)

et al. 2001

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“…In Figure , we show the list of the C α ‐tetrasubstituted α‐amino acids (both achiral and chiral) with at least two carbon atoms in each side chain and without C α i ↔ C α i cyclization investigated to date, the homo‐peptides of which are known to largely result in the 2.0 5 ‐helix structure …”

Section: Resultsmentioning

confidence: 99%

“…The highly crystalline nature of model peptides based on the subclass of C α ‐tetrasubstituted residues shown in Figure was exploited by our and a few other groups for extensive crystallographic investigations …”

Section: Resultsmentioning

confidence: 99%

“…About 10 structures of linear peptides containing Dϕg, the most hindered residue of this subclass were solved by X‐ray diffraction . In almost all of them, Dϕg is fully‐extended (although sometimes distorted).…”

Section: Resultsmentioning

confidence: 99%

“…In Figure the 3D‐structure of the terminally protected Dϕg homo‐trimer is shown . All three residues adopt a C 5 conformation, but the ψ 2 torsion angle is severely distorted (157.3 ° ).…”

Section: Resultsmentioning

confidence: 99%

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Multiple, consecutive, fully‐extended 2.0₅‐helix peptide conformation

et al. 2013

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The peptide 2.0(5)-helix does exist. It has been experimentally authenticated both in the crystalline state (by X-ray diffraction) and in solution (by several spectroscopic techniques). It is the most common conformation for C(α)-tetrasubstituted α-amino acids with at least two atoms in each side chain, provided that cyclization on the C(α)-atom is absent. X-Ray diffraction has allowed a detailed description of its geometrical and three-dimensional (3D)-structural features. The infrared absorption and the nuclear magnetic resonance parameters characteristics of this multiple, consecutive, fully-extended structure have been described. Conformational energy calculations are in agreement with the experimental findings. As the contribution per amino acid residue to the length of this helix is the longest possible, its exploitation as a molecular spacer is quite promising. However, it is a rather fragile 3D-structure and particularly sensitive to solvent polarity. Interestingly, in such a case, it may reversibly convert to the much shorter 3(10)-helix, thus generating an attractive molecular spring.

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The 2.0₅‐helix in hetero‐oligopeptides entirely composed of C^α,α‐disubstituted glycines with both side chains longer than methyls

et al. 2014

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The existence of the very uncommon, but potentially quite interesting, multiple, consecutive fully-extended conformation (2.0₅-helix) has been already clearly demonstrated in homo-oligopeptides based on quaternary α-amino acids with both side chains longer than methyls, but not cyclized on the α-carbon atom. To extend the scope of this research, in this work we investigated the occurrence of this flat 3D-structure in hetero-oligopeptides, each composed of two or three different residues of that class. The synthesis of a terminally protected peptide series to the tetrapeptide level was carried out by solution methods. The resulting oligomers were chemically and conformationally characterized. The data obtained point to an overwhelming population of the fully-extended conformation in CDCl3. However, a solvent-driven switch to a predominant 3₁₀-helical structure was seen in CD3CN. A delicate, local balance between these two conformations is confirmed to occur in the crystalline state. Molecular dynamics simulations in CHCl3 on a hetero-tetrapeptide converged to the fully-extended conformation even starting from the 3₁₀-helical structure.

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Conformational behavior of Cα,α-diphenyl glycine: Extended conformation in tripeptides containing consecutive Dφg residues

Cited by 6 publications

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Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)

Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)

Multiple, consecutive, fully‐extended 2.0₅‐helix peptide conformation

The 2.0₅‐helix in hetero‐oligopeptides entirely composed of C^α,α‐disubstituted glycines with both side chains longer than methyls

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Conformational behavior of Cα,α-diphenyl glycine: Extended conformation in tripeptides containing consecutive Dφg residues

Cited by 6 publications

References 0 publications

Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)

Control of peptide conformation by the Thorpe-Ingold effect (C?-tetrasubstitution)

Multiple, consecutive, fully‐extended 2.05‐helix peptide conformation

The 2.05‐helix in hetero‐oligopeptides entirely composed of Cα,α‐disubstituted glycines with both side chains longer than methyls

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Multiple, consecutive, fully‐extended 2.0₅‐helix peptide conformation

The 2.0₅‐helix in hetero‐oligopeptides entirely composed of C^α,α‐disubstituted glycines with both side chains longer than methyls