Microwave assisted wolff rearrangement: A facile method for the synthesis of Fmoc-β-amino acids

Patil, Basanagoud S.; Vasanthakumar, Ganga-Ramu; Babu, Vommina V. Suresh

doi:10.1007/bf02538389

Cited by 4 publications

(4 citation statements)

References 21 publications

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“…The synthesis of d ‐β 3 ‐amino acid Fmoc‐ d ‐β 3 ‐6,6‐diiodo‐allylhomoglycine ( 8 ) suitable for the synthesis of β‐peptides, was based on the respective α‐amino acid preparation (Scheme ). Compared with Fmoc‐5,5‐diiodoallylglycine, which was reported previously, the d ‐β 3 ‐amino acid has one additional CH 2 group that was introduced by an optimized Arndt–Eistert homologation method . Boc‐ d ‐β 3 ‐Asp‐OBzl ( 1 ) was obtained starting from Boc‐ l ‐Asp(OBzl)‐OH.…”

Section: Resultsmentioning

confidence: 99%

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Heavy‐Atom Labeled Transmembrane β‐Peptides: Synthesis, CD‐Spectroscopy, and X‐ray Diffraction Studies in Model Lipid Multilayer

Rost

Salditt

et al. 2016

ChemPhysChem

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Transmembrane β-peptides are promising candidates for the design of well-controlled membrane anchors in lipid membranes. Here, we present the synthesis of transmembrane β-peptides with and without tryptophan anchors, as well as a novel iodine-labeled d-β(3) -amino acid. By using one or more of the heavy-atom labeled amino acids as markers, the orientation of the helical peptide was inferred based on the electron-density profile determined by X-ray reflectivity. The β-peptides were synthesized through manual Fmoc-based solid-phase peptide synthesis (SPPS) and reconstituted in unilamellar vesicles forming a right-handed 314 -helix secondary structure, as shown by circular dichroism spectroscopy. We then integrated the β-peptide into solid-supported membrane stacks and carried out X-ray reflectivity and grazing incidence small-angle X-ray scattering to determine the β-peptide orientation and its effect on the membrane bilayers. These β-peptides adopt a well-ordered transmembrane motif in the solid-supported model membrane, maintaining the basic structure of the original bilayer with some distinct alterations. Notably, the helical tilt angle, which accommodates the positive hydrophobic mismatch, induces a tilt of the acyl chains. The tilted chains, in turn, lead to a membrane thinning effect.

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Section: Resultsmentioning

confidence: 99%

“…The required d ‐β 3 ‐amino acid derivatives 1 – 4 were synthesized by an optimized Arndt–Eistert homologation method and were used without further purification . β‐Peptides 9 – 14 were synthesized by using manual microwave‐assisted Fmoc‐based solid‐phase peptide synthesis (Fmoc‐SPPS) on a rink‐amid MBHA resin .…”

Section: Methodsmentioning

confidence: 99%

Heavy‐Atom Labeled Transmembrane β‐Peptides: Synthesis, CD‐Spectroscopy, and X‐ray Diffraction Studies in Model Lipid Multilayer

Rost

Salditt

et al. 2016

ChemPhysChem

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“…D-β 3 -Amino acids were readily prepared in very good yields from their D-α-amino acid counterparts through Arndt-Eistert homologation. [78,138,150,151] This method leaves the stereocenter at the α-carbon intact and precisely inserts a CH2-group into the amino acid backbone.…”

Section: Synthesis Of D-β 3 -Amino Acidsmentioning

confidence: 99%

“…The β 3 -D-amino acids (β 3 -AA) used in this work were obtained from their corresponding αamino acids using Arndt-Eistert homologation intermediated by Wolff rearrangement. [78,150] Scheme 6.1. Schematic presentation for the synthesis of β 3 -D-amino acids.…”

Section: Synthesis Of β 3 -D-amino Acidsmentioning

confidence: 99%

Dynamics, Intermolecular Interactions, and Organization of Transmembrane β-Peptides

Zanbot¹

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Cellular membranes contain a vast variety of proteins, which are practically required for every vital mechanism, such as selective transportation of ions and organic molecules, cell-cell recognition and signal transduction. [1] Nowadays, the major concern in life science is to gather an overview about the thermodynamics and kinetics that govern the native folding and aggregational behavior of these proteins. Artificially folded polymers, or foldamers, have attracted the interest of many research groups since they showed the potential for considerable versatilityin biological functions akin to natural proteins. [2] Thus, the prudent preorganization and refinement of such molecules can shed light on the molecular forces that control the structural features of membrane proteins and thereby, explore the correlation between their conformational stability and biological activity.In particular, β-peptides have recently been used as very promising peptide mimics with interesting conformational and functional propensities. These non-biological polymers are stable towards enzymatic degradation and they can fold into compact multihelical structures including the 14-and the 12-helix. [3] Generally, introducing non-covalent interactions, such as hydrogen bonds and Vander Waals forces via interhelical side chains can enhance the threedimensional stability of proteins. In this regard, β-peptides have been largely utilized as suitable folding patterns to provide information about self-assembly processes.

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Green synthesis and properties of arginine derived complexes for assorted drug delivery systems: A review

Patel

Dholakia

et al. 2021

Sustainable Chemistry and Pharmacy

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Microwave assisted wolff rearrangement: A facile method for the synthesis of Fmoc-β-amino acids

Cited by 4 publications

References 21 publications

Heavy‐Atom Labeled Transmembrane β‐Peptides: Synthesis, CD‐Spectroscopy, and X‐ray Diffraction Studies in Model Lipid Multilayer

Heavy‐Atom Labeled Transmembrane β‐Peptides: Synthesis, CD‐Spectroscopy, and X‐ray Diffraction Studies in Model Lipid Multilayer

Dynamics, Intermolecular Interactions, and Organization of Transmembrane β-Peptides

Green synthesis and properties of arginine derived complexes for assorted drug delivery systems: A review

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