The synthesis of Fmoc-O-allyl β-serine

Bergman, Ylva Elisabet; Ciampini, Marisa; Jalal, Sania; Lagiakos, Helen Rachel; Aguilar, Marie Isabel; Perlmutter, Patrick

doi:10.1016/j.tetasy.2008.12.022

Tetrahedron: Asymmetry

2008

DOI: 10.1016/j.tetasy.2008.12.022

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The synthesis of Fmoc-O-allyl β-serine

Ylva Elisabet Bergman¹,

Marisa Ciampini²,

Sania Jalal³

et al.

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Cited by 3 publications

(3 citation statements)

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“…The CD spectra of 1 and 4 in MeOH (Fig. 2, a) show curves characteristic of 3 14 hSer residues. Significantly, this enhanced effect is also apparent in H 2 O with maximum negative mean molar ellipticities of À 5000 and À 15000 observed for 1 and 4, respectively.…”

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confidence: 98%

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Synthesis and High‐Resolution NMR Structure of a β³‐Octapeptide with and without a Tether Introduced by Olefin Metathesis

Ebert

Gardiner

Ballet

et al. 2009

Helvetica Chimica Acta

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Bridging between (i)-and (i þ 3)-positions in a b3 -peptide with a tether of appropriate length is expected to prevent the corresponding 3 14 -helix from unfolding ( hIle-OH (1; with allylated bhSer residues in 3-and 6-position), and three tethered b-peptides 2 -4 (related to 1 through ring-closing metathesis) have been synthesized (solid-phase coupling, Fmoc strategy, on chlorotrityl resin; Scheme). A comparative CD analysis of the tethered b-peptide 4 and its non-tethered analogue 1 suggests that helical propensity is significantly enhanced (threefold CD intensity) by a (CH 2 ) 4 linker between the b 3 hSer side chains (Fig. 2). This conclusion is based on the premise that the intensity of the negative Cotton effect near 215 nm in the CD spectra of b 3 -peptides represents a measure of helical content. An NMR analysis in CD 3 OH of the two b 3 -octapeptide derivatives without (i.e., 1) and with tether (i.e., 4; Tables 1 -6, and Figs. 4 and 5) provided structures of a degree of precision (by including the complete set of side chainside chain and side chain -backbone NOEs) which is unrivaled in b-peptide NMR-solution-structure determination. Comparison of the two structures (Fig. 5) reveals small differences in side-chain arrangements (separate bundles of the ten lowest-energy structures of 1 and 4, Fig. 5, A and B) with little deviation between the two backbones (superposition of all structures of 1 and 4, Fig. 5, C). Thus, the incorporation of a CH 2 ÀOÀ(CH 2 ) 4 ÀOÀCH 2 linker between the backbone of the b 3 -amino acids in 3-and 6-position (as in 4) does accurately constrain the peptide into a 3 14 -helix. The NMR analysis, however, does not suggest an increase in the population of a 3 14 -helical backbone conformation by this linkage. Possible reasons for the discrepancy between the conclusion from the CD spectra and from the NMR analysis are discussed.

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mentioning

confidence: 98%

“…The synthesis of the peptides 1 -4 involved an on-bead strategy with incorporation of two O-allyl-b 3 hSer residues [14] for subsequent RCM (Scheme). Removal of the onbead assembled peptide from the resin with simultaneous deprotection of the sidechain protecting groups under standard conditions gave the linear b 3 -octapeptide derivative 1.…”

mentioning

confidence: 99%

Synthesis and High‐Resolution NMR Structure of a β³‐Octapeptide with and without a Tether Introduced by Olefin Metathesis

Ebert

Gardiner

Ballet

et al. 2009

Helvetica Chimica Acta

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“…We chose to study hexa-β-peptides 1a − 1d as our RCM precursor candidates (Scheme ). In each case, two β 3 -serines bearing an O -allyl side chain are located in an i /( i +3) relationship.…”

mentioning

confidence: 99%

Synthesis of Stapled β³-Peptides through Ring-Closing Metathesis

et al. 2009

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The first synthesis of carbon-stapled beta(3)-peptides is reported. The precursor beta(3)-peptides, with O-allyl beta-serines located in an i/i+3 relationship, were prepared on solid phase. We show that efficient ring-closing metathesis (RCM) of these new beta(3)-peptides proceeds smoothly either in solution or on an appropriate solid support. All products were generated with high selectivity for the E-isomer.

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Self-assembled ion-pair organocatalysis – asymmetric Baeyer–Villiger oxidation mediated by flavinium–cinchona alkaloid dimer

2016

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An ion-pair catalyst generated by assembly of a chiral flavinium and a cinchona alkaloid dimer for use in asymmetric Baeyer-Villiger oxidation is presented. Ion-pair formation is essential for enhancing the catalytic activity and stereoselectivity. The catalyst is applicable to structurally diverse 3-substituted cyclobutanones, providing good to excellent enantioselectivities (up to 98 : 2 e.r.). This study provides the first example of self-assembly of a flavin derivative and a base to form a chiral reaction site that enables a highly stereoselective reaction to occur.

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The synthesis of Fmoc-O-allyl β-serine

Cited by 3 publications

References 9 publications

Synthesis and High‐Resolution NMR Structure of a β³‐Octapeptide with and without a Tether Introduced by Olefin Metathesis

Synthesis and High‐Resolution NMR Structure of a β³‐Octapeptide with and without a Tether Introduced by Olefin Metathesis

Synthesis of Stapled β³-Peptides through Ring-Closing Metathesis

Self-assembled ion-pair organocatalysis – asymmetric Baeyer–Villiger oxidation mediated by flavinium–cinchona alkaloid dimer

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The synthesis of Fmoc-O-allyl β-serine

Cited by 3 publications

References 9 publications

Synthesis and High‐Resolution NMR Structure of a β3‐Octapeptide with and without a Tether Introduced by Olefin Metathesis

Synthesis and High‐Resolution NMR Structure of a β3‐Octapeptide with and without a Tether Introduced by Olefin Metathesis

Synthesis of Stapled β3-Peptides through Ring-Closing Metathesis

Self-assembled ion-pair organocatalysis – asymmetric Baeyer–Villiger oxidation mediated by flavinium–cinchona alkaloid dimer

Contact Info

Product

Resources

About

Synthesis and High‐Resolution NMR Structure of a β³‐Octapeptide with and without a Tether Introduced by Olefin Metathesis

Synthesis and High‐Resolution NMR Structure of a β³‐Octapeptide with and without a Tether Introduced by Olefin Metathesis

Synthesis of Stapled β³-Peptides through Ring-Closing Metathesis