Chemoenzymatic synthesis of Fmoc-protected (2S,3S)-2-hydroxy-3-amino acids and their application in the synthesis of an α-hydroxylated β-hexapeptide

Tromp, Reynier A.; Hoeven, Michael van der; Amore, Alessia; Brussee, Johannes; Overhand, Mark; Marel, Gijs A. van der; Gen, A. Van Der

doi:10.1016/s0957-4166(01)00193-8

Cited by 20 publications

(12 citation statements)

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“…Due to the recent extensive research in the field of β‐peptides, both experimental and theoretical methods have revealed that they may exhibit numerous secondary structure elements 1–27. Several helices,1–10 turns,9, 11 polar, and nonpolar sheet‐ or strand‐like foldings12–16 were assigned. Similarly, models composed of both α‐ and β‐amino acid residues have resulted in distinct folds 17–19.…”

Section: Introductionmentioning

confidence: 99%

Toward a rational design of β‐peptide structures

2005

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Intrinsic conformational characteristics of beta-peptides built up from simple achiral and chiral beta-amino acid residues (i.e., HCO-beta-Ala-NH2, HCO-beta-Abu-NH2) were studied using quantum chemical calculations and 1H-NMR spectroscopy. A conformer-based systematic and uniform nomenclature was introduced to differentiate conformers. Geometry optimizations were performed on all homoconformers of both HCO-(beta-Ala)(k)-NH2 and HCO-(beta-Abu)(k)-NH2 (1 < or = k < or = 6) model systems at the RHF/3-21G and RHF/6-311++G(d, p) levels of theory. To test for accuracy and precision, additional computations were carried out at several levels of theory [e.g., RHF/6-31G(d), and B3LYP/6-311++G(d, p)]. To display the folding preference, the relative stability of selected conformers as function of the length of the polypeptide chain was determined. Ab initio population distribution of hexapeptides and the conformational ensemble of synthetic models composed of beta-Ala and beta-Abu studied using 1H-NMR in different solvents were compared at a range of temperatures. Helical preference induced by various steric effects of nonpolar side chains was tested using higher level ab initio methods for well-known model systems such as: HCO-(beta-HVal-beta-HAla-beta-HLeu)2-NH2, HCO-(ACHC)6-NH2, HCO-(trans-ACPC)6-NH2, and HCO-(cis-ACPC)6-NH2. The relative stabilities determined by theoretical methods agreed well with most experimental data, supporting the theory that the local conformational preference influenced by steric effects is a key determining factor of the global fold both in solution and in the gas phase.

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Section: Introductionmentioning

confidence: 99%

Toward a rational design of β‐peptide structures

2005

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“…In 2001, Tromp et al preparedhydroxylated -oligopeptides, starting from -hydroxylated -alanine, -valine and -leucine, in solid phase syntheses. NMR studies on the resulting -hydroxylated -hexapeptide gave strong indications that in pyridine no helical structure was formed [21]. In contrast, in 2002 Gellman et al reported that oligomers composed of 3-methoxy-or 3-phenoxysubstituted trans-2-aminocyclopentanecarboxylic acid (ACPC) residues maintain the 12-helical conformation displayed by the nonsubstituted analogs [22].…”

Section: Introductionmentioning

confidence: 99%

Syntheses of Hydroxylated Cyclic β-Amino Acid Derivatives

Palkó

Kiss²,

Fülöp

2005

CMC

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This review is intended to give a short summary of the developments in the field of natural and synthetic alicyclic and heterocyclic hydroxylated beta-amino acids and to focus on the main strategies that have been reported for their synthesis. Given the medicinal and biological significance of the hydroxylated beta-amino acids, an increasing volume of research is currently being directed toward regio-, stereo- and enantioselective access to this class of compounds.

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“…[7] Tromp et al prepared an oligomer containing residues, which are diastereoisomers of E, but did not report conclusive evidence for its conformation. [8] We became interested in synthesizing the b-hexapeptide 1 to study the conformational consequences of the attachment of heteroatoms directly to the peptidic backbone. [9,10] The relative configuration unlike was chosen which should prevent folding to the 3 14 -helix: Notably, the analogous compound (cf.…”

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confidence: 99%

The Fourth Helical Secondary Structure of β‐Peptides: The (P)‐2₈‐Helix of a β‐Hexapeptide Consisting of (2R,3S)‐3‐Amino‐2‐hydroxy Acid Residues

Gademann¹,

Häne²,

Rueping³

et al. 2003

Angew Chem Int Ed

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Chemoenzymatic synthesis of Fmoc-protected (2S,3S)-2-hydroxy-3-amino acids and their application in the synthesis of an α-hydroxylated β-hexapeptide

Cited by 20 publications

References 27 publications

Toward a rational design of β‐peptide structures

Toward a rational design of β‐peptide structures

Syntheses of Hydroxylated Cyclic β-Amino Acid Derivatives

The Fourth Helical Secondary Structure of β‐Peptides: The (P)‐2₈‐Helix of a β‐Hexapeptide Consisting of (2R,3S)‐3‐Amino‐2‐hydroxy Acid Residues

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Chemoenzymatic synthesis of Fmoc-protected (2S,3S)-2-hydroxy-3-amino acids and their application in the synthesis of an α-hydroxylated β-hexapeptide

Cited by 20 publications

References 27 publications

Toward a rational design of β‐peptide structures

Toward a rational design of β‐peptide structures

Syntheses of Hydroxylated Cyclic β-Amino Acid Derivatives

The Fourth Helical Secondary Structure of β‐Peptides: The (P)‐28‐Helix of a β‐Hexapeptide Consisting of (2R,3S)‐3‐Amino‐2‐hydroxy Acid Residues

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The Fourth Helical Secondary Structure of β‐Peptides: The (P)‐2₈‐Helix of a β‐Hexapeptide Consisting of (2R,3S)‐3‐Amino‐2‐hydroxy Acid Residues