Conformational study of poly‐ΔAbu peptides and construction of amphipathic nanostructure

Nandel, Fateh S.; Sahrawat, Tammanna R.

doi:10.1002/bip.21118

Cited by 5 publications

(4 citation statements)

References 60 publications

(63 reference statements)

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“…a,b-Dehydroamino acids are non-proteinogenic residues often found in natural products produced by microorganisms, marine organisms and plants. 1 Dehydroamino acids usually exist as the Z-isomer as it is thermodynamically more stable than the Eisomer. [1][2][3][4] The E-and Z-isomers of certain dehydroamino acids, such as dehydrophenylalanine and dehydrotryptophan, are able to interconvert photochemically, either when incorporated into peptides or as part of smaller derivatives.…”

Section: Introductionmentioning

confidence: 99%

“…1 Dehydroamino acids usually exist as the Z-isomer as it is thermodynamically more stable than the Eisomer. [1][2][3][4] The E-and Z-isomers of certain dehydroamino acids, such as dehydrophenylalanine and dehydrotryptophan, are able to interconvert photochemically, either when incorporated into peptides or as part of smaller derivatives. 4, 5 The E/Z configuration of the double bond affects the conformation of dehydroamino acid containing peptides, and hence the biological activity of these compounds.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The synthesis of dehydrotryptophan and dehydrotryptophan-containing peptides

Kaur¹,

Heapy²,

Brimble³

2011

Org. Biomol. Chem.

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Dehydrotryptophan and its derivatives are non-proteinogenic amino acids commonly found in peptide-based natural products produced by microorganisms, marine organisms and plants. These non-proteinogenic amino acids are found in secondary metabolites and are formed by post translational modification processes. Although comprehensive reviews on the synthesis of dehydroamino acids are available, this perspective focuses solely on methods to synthesise the dehydrotryptophan-containing segment of naturally occurring peptides, amino acids and their derivatives.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The synthesis of dehydrotryptophan and dehydrotryptophan-containing peptides

Kaur¹,

Heapy²,

Brimble³

2011

Org. Biomol. Chem.

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“…The conformational properties of peptides carrying α,β-dehydroamino acids have been extensively reviewed in the past [ 112 , 113 , 114 , 115 , 116 , 117 , 118 ] but remain a hot topic today [ 119 , 120 , 121 ]. The residues dehydroalanine (ΔAla), dehydrobutyrine (ΔAbu), and dehydrophenylalanine (ΔPhe) are the most investigated [ 122 , 123 , 124 , 125 , 126 , 127 , 128 ]. ΔPhe has been intensively studied computationally [ 129 , 130 ].…”

Section: Peptidomimetics Designmentioning

confidence: 99%

Non-Canonical Amino Acids as Building Blocks for Peptidomimetics: Structure, Function, and Applications

et al. 2023

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This review provides a fresh overview of non-canonical amino acids and their applications in the design of peptidomimetics. Non-canonical amino acids appear widely distributed in nature and are known to enhance the stability of specific secondary structures and/or biological function. Contrary to the ubiquitous DNA-encoded amino acids, the structure and function of these residues are not fully understood. Here, results from experimental and molecular modelling approaches are gathered to classify several classes of non-canonical amino acids according to their ability to induce specific secondary structures yielding different biological functions and improved stability. Regarding side-chain modifications, symmetrical and asymmetrical α,α-dialkyl glycines, Cα to Cα cyclized amino acids, proline analogues, β-substituted amino acids, and α,β-dehydro amino acids are some of the non-canonical representatives addressed. Backbone modifications were also examined, especially those that result in retro-inverso peptidomimetics and depsipeptides. All this knowledge has an important application in the field of peptidomimetics, which is in continuous progress and promises to deliver new biologically active molecules and new materials in the near future.

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“…It has been shown recently, though, that poly-∆Abu exists in alternate ∆ Z Abu and ∆ E Abu form rather than the all Zform. 1 A great majority of papers published so far on dehydropeptides deal with ∆-amino acid residues of the Z configuration. The most studied dehydroamino acid residue has been dehydrophenylalanine.…”

Section: Introductionmentioning

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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Conformational study of poly‐ΔAbu peptides and construction of amphipathic nanostructure

Cited by 5 publications

References 60 publications

The synthesis of dehydrotryptophan and dehydrotryptophan-containing peptides

The synthesis of dehydrotryptophan and dehydrotryptophan-containing peptides

Non-Canonical Amino Acids as Building Blocks for Peptidomimetics: Structure, Function, and Applications

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

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