A helical Dpg homo-peptide

Blasio, Benedetto Di; Pavone, Vincenzo; Isernia, Carla; Pedone, Carlo; Benedetti, Ettore; Toniolo, Claudio; Hardy, P. M.; Lingham, Ian N.

doi:10.1039/p29920000523

Cited by 23 publications

(15 citation statements)

References 13 publications

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“…However, more recently, detailed energy computations and x‐ray diffraction and solution conformational investigations have shown that the picture presented above is not so simple, in that Deg, Dp n g, Db

_{n}^{u}

g, Dvg ( C α,α ‐divinylglycine), Dp r g ( C α,α ‐dipropargylglycine), and Dp c g ( C α,α ‐dicyclopropylglycine) (Figure 1) rich peptides can adopt either the fully extended or the helical conformation depending upon physical state (including solvent polarity) and sequence context, thus emphasizing that energy differences between these two structures, at least at the level of these residues, are small 71–90. The delicate balance between the two conformations has been confirmed by incorporation in a host sequence of a modest point defect [an Abu guest residue perturbing the regular alignment of the side chain of a (Deg) 5 homo peptide], which is enough to drastically bias the preferred conformation toward the 3 10 ‐helix 91.…”

Section: Discussionmentioning

confidence: 99%

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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Section: Discussionmentioning

confidence: 99%

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

et al. 2001

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“…89 Interestingly even in the homotripeptide Tfa-(Dpg) 3 -DBH (DBH= N,N(-dibenzyl-hydrazide), all the three Dpg residues adopt helical f, c values. 90 Recent studies from our laboratory have attempted to probe the eect of local sequence variations on Dpg residue conformation.…”

Section: ±85mentioning

confidence: 99%

Stereochemical Control of Peptide Folding

Kaul

Balaram

1999

Bioorganic & Medicinal Chemistry

153

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AbstractÐStereochemically constrained amino acid residues that strongly favour speci®c backbone conformations may be used to nucleate and stabilize speci®c secondary structures in designed peptides. An overview of the use of aa-dialkyl amino acids in stabilizing helical structures in synthetic peptides is presented, with an emphasis on work carried out in the authors laboratory. a-Aminoisobutyric acid (Aib) and related achiral homologs facilitate stable helix formation in oligopeptides as exempli®ed by a large number of crystal structure determinations in the solid state. The ability to design conformationally rigid helical modules has been exploited in attempts to design structurally well characterized helix-linker±helix, using potential nonhelical linking segments. bHairpin design has been approached by exploiting the tendency of`prime turns' to nucleate hairpin formation. The use of nucleating D Pro-Gly segments has resulted in the generation of several well characterized b-hairpin structures, including the crystallographic observation of b-hairpin in a synthetic apolar octapeptide. Extensions of this approach to three stranded b-sheets and larger structures containing multiple D Pro-Gly segments appear readily possible.

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“…It has been reported that, with a few exceptions, 28,[52][53][54] extended conformations are favored over helical conformations when the C ␣ atom is symmetrically disubstituted with linear alkyl side chains, such as in Deg and Dpg. 23,55 On the opposite side, the helical conformation becomes more stable when the side chains are interconnected into a cyclic system, as for the cycloaliphatic residues of general formula Ac n c, with n ϭ 5, 6, 7.…”

Section: Discussionmentioning

confidence: 99%

“…21,22 In the last few years we devoted our attention to the conformational behavior of new C ␣,␣ -dialkylated residues, containing different groups of increasing bulkiness on the C ␣ atom. [23][24][25][26][27][28] In particular, the conformational preferences of Dg (C ␣,␣ -diphenylglycine) containing peptides have been recently analyzed. 29 -36 As a part of this program, we have now undertaken the study of the conformational properties of the Afc residue, which can be considered as a Dg derivative, since it contains on the C ␣ atom two phenyl rings condensed through their orto positions.…”

Section: Introductionmentioning

confidence: 99%