Phosphonic analogues of tyrosine and 3,4-dihydroxyphenylalanine (dopa) influence mushroom tyrosinase activity

Lejczak, Barbara; Kafarski, Paweł; Makowiecka, E

doi:10.1042/bj2420081

Cited by 33 publications

(14 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Notably, the latter can provide convenient access [15] to important phosphorus analogues of phenylalanine (A), tyrosine (B) or DOPA (C). [16] In this full account we report a detailed study of the application of phosphane-phosphite (P-OP) ligands to the enantioselective hydrogenation of enol-ester phosphonates in studies including the synthesis of new ligands and catalyst precursors, supplemented with X-ray and NMR structural data for pertinent rhodium complexes. Part of this work has been published in a preliminary form.…”

Section: Introductionmentioning

confidence: 99%

Tuning of the Structures of Chiral Phosphane‐Phosphites: Application to the Highly Enantioselective Synthesis of α‐Acyloxy Phosphonates by Catalytic Hydrogenation

Rubio

Vargas

Suárez

et al. 2007

Chemistry A European J

View full text Add to dashboard Cite

A family of new chiral phosphane-phosphites 5 has been prepared and employed in the synthesis of rhodium complexes of formulation [Rh(cod)(5)]BF4 (7). The use of bulky phosphane or phosphite groups in the preparation of 7 avoids the formation of undesired disubstituted complexes, one of which (9 a) has been isolated and characterized. Ligands 5 display important differences from the bulkier phosphane-phosphites 1: complexes 7-unlike their rigid [Rh(cod)(1)]BF4 counterparts-show fluxional behaviour in solution, consistent with backbone oscillation around the coordination plane. A detailed screening of ligands 1 and 5 in catalytic asymmetric hydrogenations of enol phosphonates 12 demonstrated a critical influence of the steric characteristics of the phosphane-phosphite in the course of the reaction, and optimization of the two phosphorus functionalities resulted in the production of versatile and efficient catalysts for this class of hydrogenations: enantioselectivities of up to 98% ee were thus obtained with substrates bearing an alkyl substituent in the beta-position, while for their challenging aryl counterparts values of up to 92% ee were achieved. The coordination mode of phosphonate 12 a towards a Rh phosphane-phosphite fragment has also been investigated and a preference of the olefin fragment to occupy the position cis to the phosphite group has been observed. From this observation an interpretation of the configurations of the hydrogenated phosphonates has also been made.

show abstract

Section: Introductionmentioning

confidence: 99%

Tuning of the Structures of Chiral Phosphane‐Phosphites: Application to the Highly Enantioselective Synthesis of α‐Acyloxy Phosphonates by Catalytic Hydrogenation

Rubio

Vargas

Suárez

et al. 2007

Chemistry A European J

View full text Add to dashboard Cite

show abstract

“…Some of the most potent, competitive inhibitors include mimosine [5,6], tropolone [7,8], and kojic acid [9–12]. Some of us had previously shown that amino‐(3,4‐dihydroxyphenyl)methylphosphonic acid, the phosphonic analog of 3,4‐dihydroxyphenylglycine, was also a potent inhibitor of tyrosinase [13]. With a K i of 50 and 97 µ m for tyrosine and Dopa as substrates, respectively, it was comparable with mimosine and tropolone.…”

mentioning

confidence: 99%

Redox reaction between amino‐(3,4‐dihydroxyphenyl)methyl phosphonic acid and dopaquinone is responsible for the apparent inhibitory effect on tyrosinase

Gąsowska¹,

Wojtasek²,

Hurek³

et al. 2002

European Journal of Biochemistry

View full text Add to dashboard Cite

Amino-(3,4-dihydroxyphenyl)methyl phosphonic acid, the phosphonic analog of 3,4-dihydroxyphenylglycine, had been previously reported as a potent inhibitor of tyrosinase. The mechanism of the apparent enzyme inhibition by this compound has now been established. Amino-(3,4-dihydroxyphenyl)methyl phosphonic acid turned out to be a substrate and was oxidized to o-quinone, which evolved to a final product identified as 3,4-dihydroxybenzaldehyde, the same as for 3,4-dihydroxyphenylglycine. Monohydroxylated compounds (amino-(3-hydroxyphenyl)methyl phosphonic acid and amino-(4-hydroxyphenyl)methyl phosphonic acid) were not oxidized, neither was 4-hydroxy-L-phenylglycine. However, the relatively high K m for amino-(3,4-dihydroxyphenyl)methyl phosphonic acid (0.52 mM) indicated that competitive inhibition could not entirely explain the previously reported strong inhibitory effect (K i ¼ 50 and 97 lM for tyrosine and 3-(3,4-dihydroxyphenyl)alanine (Dopa) as substrates, respectively). Neither was the enzyme covalently inactivated to a significant degree. Spectroscopic and electrochemical analysis of the oxidation of a mixture of Dopa and the inhibitor demonstrated that the phosphonic compound reduced dopaquinone back to Dopa, thus diminishing and delaying the formation of dopachrome. This produces an apparent strong inhibitory effect when the reaction is monitored spectrophotometrically at 475 nm. In this peculiar case Dopa acts as a redox shuttle mediating the oxidation of the shorter phosphonic homolog. Decomposition of the phosphonic o-quinone to 3,4-dihydroxybenzaldehyde drives the reaction against the slightly unfavorable difference in redox potentials.Keywords: tyrosinase; redox exchange; quinone; phosphonic amino acids; 3,4-dihydroxybenzaldehyde.Tyrosinase (EC 1.14.18.1) is a copper-containing enzyme widely distributed in nature. It catalyses the hydroxylation of monophenols to o-diphenols and the oxidation of the latter to o-quinones using molecular oxygen. Its action on the physiological substrate, L-tyrosine, produces L-3-(3,4-dihydroxyphenyl)alanine (L-Dopa) and then dopaquinone, which undergoes a series of nonenzymatic reactions leading to melanins [1]. The enzyme is responsible for melanization in animals and browning in plants. As browning in food products is an undesirable process, there has been a constant need in food industry for compounds preventing this reaction. Inhibition of mammalian tyrosinase has also been indicated as a possible approach to control human melanoma [2]. Although a large number of tyrosinase inhibitors have been described in the literature [3], the search for new natural products and synthetic compounds with such activity still continues [4]. Some of the most potent, competitive inhibitors include mimosine [5,6], tropolone [7,8], and kojic acid [9][10][11][12]. Some of us had previously shown that amino-(3,4-dihydroxyphenyl)methyl phosphonic acid, the phosphonic analog of 3,4-dihydroxyphenylglycine, was also a potent inhibitor of tyrosinase [13]. With a K i of 50 and 97 lM for tyrosin...

show abstract

“…Most investigations on interactions of phosphonic acid derivatives with tyrosinase reported in the literature [38][39][40] regards structures which are analogs of tyrosinase natural substrates: L-Tyrosine and L-DOPA and they contain phenolic or diphenolic moiety. Some of the compounds acted as tyrosinase new substrates and some revealed moderate inhibitory activity.…”

Section: Discussionmentioning

confidence: 99%

Phosphonic and Phosphinic Acid Derivatives as Novel Tyrosinase Inhibitors: Kinetic Studies and Molecular Docking

Wolińska

Hałdys

Góra

et al. 2019

Chemistry & Biodiversity

View full text Add to dashboard Cite

A dozen of phosphonic and phosphinic acid derivatives containing pyridine moiety were synthesized and its inhibitory activity toward mushroom tyrosinase was investigated. Moreover, molecular docking of these compounds to the active site of the enzyme was performed. All the compounds (1–10) demonstrated the inhibitory effect with the IC50 and inhibition constants ranging millimolar concentrations. The obtained results indicate that the compounds show different types of inhibition (competitive, noncompetitive, mixed), but all of them are reversible inhibitors. The obtained outcomes allowed to make the structure–activity relationship (SAR) analysis. Compound 4 ([(benzylamino)(pyridin‐2‐yl)methyl]phenylphosphinic acid) revealed the lowest IC50 value of 0.3 mm and inhibitory constant of Ki 0.076 mm, with noncompetitive type and reversible mechanism of inhibition. According to SAR analysis, introducing bulky phenyl moieties to phosphonic and amino groups plays an important role in the inhibitory potency on activity of mushroom tyrosinase and could be useful in design and development of a new class of potent organophosphorus inhibitors of tyrosinase. Combined results of molecular docking and SAR analysis can be helpful in designing novel tyrosinase inhibitors of desired properties. They may have broad application in food industry and cosmetology.

show abstract

Phosphonic analogues of tyrosine and 3,4-dihydroxyphenylalanine (dopa) influence mushroom tyrosinase activity

Cited by 33 publications

References 23 publications

Tuning of the Structures of Chiral Phosphane‐Phosphites: Application to the Highly Enantioselective Synthesis of α‐Acyloxy Phosphonates by Catalytic Hydrogenation

Tuning of the Structures of Chiral Phosphane‐Phosphites: Application to the Highly Enantioselective Synthesis of α‐Acyloxy Phosphonates by Catalytic Hydrogenation

Redox reaction between amino‐(3,4‐dihydroxyphenyl)methyl phosphonic acid and dopaquinone is responsible for the apparent inhibitory effect on tyrosinase

Phosphonic and Phosphinic Acid Derivatives as Novel Tyrosinase Inhibitors: Kinetic Studies and Molecular Docking

Contact Info

Product

Resources

About