(<i>S</i>)-ABOC: A Rigid Bicyclic β-Amino Acid as Turn Inducer

André, Christophe; Legrand, Baptiste; Deng, Cheng; Didierjean, Claude; Pickaert, Guillaume; Martinez, Jean; Averlant-Petit, Marie Christine; Amblard, Muriel; Calmès, Monique

doi:10.1021/ol203406v

Cited by 38 publications

(35 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Moreover, a strong intense band arises at 1518 cm −1 which corresponds to N−H bending vibration. These observation demonstrate that backbone of peptide 2 adopts a β‐turn type structure in CHCl 3 . The characteristic structural diversity was also evidenced from 2D‐NMR study.…”

Section: Resultssupporting

confidence: 66%

Modulating Hydrogen Bonded Self-assembled Patterns and Morphological Features by a Change in Side Chain of Third Amino Acid of Synthetic γ- Amino Acid Based Tripeptides

et al. 2016

View full text Add to dashboard Cite

Self‐assembled structure and functions of peptides could be achieved by the design and synthesis of hybrid peptides. Here, we report structural and morphological studies of designed hybrid tripeptides Boc‐Gpn‐Aib‐Xaa‐OMe (where Xaa=Leu(L) for 1 and Phe(F) for 2), which show different conformations both in solid and solution states. The conformational modulations are achieved by the design and synthesis of reported peptides 1 and 2 by suitable choice of conventional and non‐conventional amino acid building blocks and slight change in side‐chain of third amino acids of tripeptides. The conformational modulations exhibited by peptides 1 and 2 are well probed and confirmed using Single crystal XRD, FT‐IR, CD and 2D NMR studies. The morphological studies of peptides 1 and 2 show different self‐assembled morphological preferences in THF – water (1:1) under similar experimental conditions.

show abstract

Section: Resultssupporting

confidence: 66%

Modulating Hydrogen Bonded Self-assembled Patterns and Morphological Features by a Change in Side Chain of Third Amino Acid of Synthetic γ- Amino Acid Based Tripeptides

et al. 2016

View full text Add to dashboard Cite

show abstract

“…[22] It can be assumed that lower temperature coefficients values in CDCl 3 2.4 ppb/K are relatedn ot only to shielded protons buta lso to accessible ones;h ence,o nly valuess ignificantly larger than 2.4 ppb/K in CDCl 3 can be unambiguously assigned to NH protons initially shielded, which become exposed to the solventu poni ncreasing temperature. [5,23] On the other hand, low temperature coefficients in DMSO (< 5ppb/K) are relatedt oi naccessible protons to the solvent. Diluted solutions( 10 À3 m)o ft he compounds 14,15 in the deuterated solvents of choice were used to record the 1 HNMR spectra.S cheme 2r eports the temperature coefficients values expressed in Dppb/DKh ighlighted in red for CDCl 3 We also performed DMSO-titration experiments with gradual addition of DMSO to CDCl 3 solutions (10 À3 m)o ft he four diastereoisomers 14,15.F igure 3s hows the plots of the four compounds.…”

mentioning

confidence: 99%

Design, Synthesis, and Conformational Analysis of Proposed β‐Turn Mimics from Isoxazoline‐Cyclopentane Aminols

Memeo

Mella

Montagna

et al. 2015

Chemistry A European J

View full text Add to dashboard Cite

Constrained aminols from oxazanorbornene derivatives have the geometrical features to be used as β-turn inducers. Four different stereoisomers were prepared and spectroscopically characterized (MD calculations, NMR-titration and VT-NMR experiments). Temperature coefficients in DMSO are indicative for the existence of an intramolecular hydrogen bond. Chirooptical properties revealed a β-turn arrangement of all the synthesized compounds, where, depending on the absolute configuration of the cyclopentane spacer, they can be labeled as left- or right-handed turns.

show abstract

“…Since cyclic scaffolds such as proline analogues and diketopiperazine (DKP), are well known structures exhibiting turn inducer properties, we ambitioned that the 1,2,5‐Oxd skeleton could be defined as an alternative sources of turn inducer. Among the turns present in nature, the β‐turn is one of the major secondary structural element of proteins, playing an essential role in folding and in recognition . Most β‐turns contain an intramolecular hydrogen bond between the carbonyl oxygen of the first residue ( i ) and the amide NH proton of the fourth residue ( i + 3), forming a pseudo ten‐membered ring ,.…”

Section: Resultsmentioning

confidence: 99%

Oxa–diketopiperazines: Access and Conformational Analysis of Potential Turn Inducers

et al. 2017

Self Cite

View full text Add to dashboard Cite

An improvement of the 1,2,5‐oxadiazine‐3,6‐diones (Oxd) synthesis and reactivity is described in this paper. The methodology has been successfully applied to produce a library of this poorly studied scaffold, which can be considered as an oxa‐diketopiperazine (oxa‐DKP). Significantly, the first crystal structures of oxa‐DKP were obtained and compared to the diketopiperazine ring. Finally, a straightforward procedure concerning the coupling of various amino acids with oxa‐DKP heterocycles to afford original peptidomimetics was reported. The conformational analysis realized on di‐ and tripeptide analogs revealed that the oxa‐DKP skeleton exhibited remarkable β‐turn inducer properties.

show abstract

(S)-ABOC: A Rigid Bicyclic β-Amino Acid as Turn Inducer

Cited by 38 publications

References 31 publications

Modulating Hydrogen Bonded Self-assembled Patterns and Morphological Features by a Change in Side Chain of Third Amino Acid of Synthetic γ- Amino Acid Based Tripeptides

Modulating Hydrogen Bonded Self-assembled Patterns and Morphological Features by a Change in Side Chain of Third Amino Acid of Synthetic γ- Amino Acid Based Tripeptides

Design, Synthesis, and Conformational Analysis of Proposed β‐Turn Mimics from Isoxazoline‐Cyclopentane Aminols

Oxa–diketopiperazines: Access and Conformational Analysis of Potential Turn Inducers

Contact Info

Product

Resources

About