Enantioselective Synthesis of ?-amino acids: A Review

Ashfaq, Muhammad; Tabassum, Rukhsana; Ahmad, Muhammad Mahboob; Hassan, Nagina Ali; Oku, Hirosuke; Rivera, Gildardo

doi:10.4172/2161-0444.1000278

Cited by 34 publications

(11 citation statements)

References 107 publications

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“…The enantioselective synthesis of -amino acids has received great attention in recent times, 1,2 because they are used as chiral auxiliaries and catalysts in organic synthesis and as suitable building blocks for the preparation of diverse compounds of chemical and biological interest, mainly peptidomimetics that may overcome the pharmacological limitations of natural peptides. 3,[4][5][6][7]8,9,10 These systems are more resistant than -peptides to microorganisms and to protease and peptidase degradation and their conformational properties and stability facilitate their interaction with receptors and enzymes, and this usually results in improved activity.…”

Section: Introductionmentioning

confidence: 99%

Ring Closing Methatesis Mediated Synthesis of D-Galactose Derived β-Amino Acids

Fernández¹,

Fernández²,

Balo³

et al. 2020

Preprint

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The first example of a new stereocontrolled synthesis of polyhydroxylated 2-aminocyclopetanecarboxylic acids from hexoses is reported. It consists of the transformation of D-galactose derivative 5 into polysubstituted cyclopentane β-amino acid derivative 12b by means of a sequence that involves a Ring Closing Metathesis of the corresponding polysubstituted 2-methylenehept-6-ene 8b, followed by a stereocontrolled aza-Michael functionalization of the first reported polysubstituted cyclopent-1-ene-1- carboxylic acid ester 10b. Preliminary studies on peptides incorporating these alicyclic - amino acids are also reported. The incorporation of β-amino acid derivative 12b into peptides is also reported.

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Section: Introductionmentioning

confidence: 99%

Ring Closing Methatesis Mediated Synthesis of D-Galactose Derived β-Amino Acids

Fernández¹,

Fernández²,

Balo³

et al. 2020

Preprint

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“…In addition to conventional resolution methods for the preparation of enantiomeric β-amino acids and β-lactams, enzymatic strategies have also been described [ 18 , 19 , 20 ]. Our research group has also devised a number of efficient enzymatic kinetic and sequential kinetic resolution processes (acylations, deacylations and hydrolyses).…”

Section: Introductionmentioning

confidence: 99%

Efficient Enzymatic Routes for the Synthesis of New Eight-membered Cyclic β-Amino Acid and β-Lactam Enantiomers

et al. 2017

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Efficient enzymatic resolutions are reported for the preparation of new eight-membered ring-fused enantiomeric β-amino acids [(1R,2S)-9 and (1S,2R)-9] and β-lactams [(1S,8R)-3, (1R,8S)-3 (1S,8R)-4 and (1R,8S)-7], through asymmetric acylation of (±)-4 (E > 100) or enantioselective hydrolysis (E > 200) of the corresponding inactivated (±)-3 or activated (±)-4 β-lactams, catalyzed by PSIM or CAL-B in an organic solvent. CAL-B-catalyzed ring cleavage of (±)-6 (E > 200) resulted in the unreacted (1S,8R)-6, potential intermediate for the synthesis of enantiomeric anatoxin-a. The best strategies, in view of E, reaction rate and product yields, which underline the importance of substrate engineering, are highlighted.

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“…1) 22 . Consequently, various chemical processes for asymmetric C-N bond formation via conjugate addition have been developed during the past decade, using either metal catalysis or organocatalysis 23 . These methods rely on modified carbonyl compounds as acceptors, utilize amines instead of ammonia as the nitrogen nucleophiles, and require protective groups.…”

mentioning

confidence: 99%

“…These methods rely on modified carbonyl compounds as acceptors, utilize amines instead of ammonia as the nitrogen nucleophiles, and require protective groups. Therefore, problems such as the use of expensive catalysts or chiral auxiliaries, the need for protection and deprotection steps, and the use of harsh reaction conditions have made these processes expensive and increasingly unsustainable 23 . Biocatalytic routes would offer environmentally friendly options [24][25][26] , especially for hydroamination of acrylates by lyases, but ammonia lyases lack the required activity and/or regioselectivity 27 .…”

mentioning

confidence: 99%

“…Attempts to shift the α -regiochemical preference of arylalanine ammonia lyases to β -selectivity have met with some success, but the enzymes act only on cinnamate derivatives and even the best mutants have modest regioselectivity and low activity 28 . Thus, the development of efficient, sustainable and scalable processes toward enantiopure β -amino acids remains a formidable challenge 23 .…”

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confidence: 99%

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Computational redesign of enzymes for regio- and enantioselective hydroamination

et al. 2018

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Introduction of innovative biocatalytic processes offers great promise for applications in green chemistry. However, owing to limited catalytic performance, the enzymes harvested from nature's biodiversity often need to be improved for their desired functions by time-consuming iterative rounds of laboratory evolution. Here we describe the use of structure-based computational enzyme design to convert Bacillus sp. YM55-1 aspartase, an enzyme with a very narrow substrate scope, to a set of complementary hydroamination biocatalysts. The redesigned enzymes catalyze asymmetric addition of ammonia to substituted acrylates, affording enantiopure aliphatic, polar and aromatic β-amino acids that are valuable building blocks for the synthesis of pharmaceuticals and bioactive compounds. Without a requirement for further optimization by laboratory evolution, the redesigned enzymes exhibit substrate tolerance up to a concentration of 300 g/L, conversion up to 99%, β-regioselectivity >99% and product enantiomeric excess >99%. The results highlight the use of computational design to rapidly adapt an enzyme to industrially viable reactions.

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Enantioselective Synthesis of ?-amino acids: A Review

Cited by 34 publications

References 107 publications

Ring Closing Methatesis Mediated Synthesis of D-Galactose Derived β-Amino Acids

Ring Closing Methatesis Mediated Synthesis of D-Galactose Derived β-Amino Acids

Efficient Enzymatic Routes for the Synthesis of New Eight-membered Cyclic β-Amino Acid and β-Lactam Enantiomers

Computational redesign of enzymes for regio- and enantioselective hydroamination

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