L-DOPA: Difference between revisions

L-DOPA
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Molar mass	197.19 g/mol

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Latest revision as of 05:06, 21 December 2025

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<templatestyles src="smallcaps/styles.css"/>l-DOPA, also known as <templatestyles src="smallcaps/styles.css"/>l-3,4-dihydroxyphenylalanine and used medically as levodopa, is made and used as part of the normal biology of some plants^[1] and animals, including humans. Humans, as well as a portion of the other animals that utilize <templatestyles src="smallcaps/styles.css"/>l-DOPA, make it via biosynthesis from the amino acid <templatestyles src="smallcaps/styles.css"/>l-tyrosine.

<templatestyles src="smallcaps/styles.css"/>l-DOPA is the precursor to the neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline), which are collectively known as catecholamines. Furthermore, <templatestyles src="smallcaps/styles.css"/>l-DOPA itself mediates neurotrophic factor release by the brain and central nervous system.^[2]^[3] In some plant families (of the order Caryophyllales), <templatestyles src="smallcaps/styles.css"/>l-DOPA is the central precursor of a biosynthetic pathway that produces a class of pigments called betalains.^[4]

<templatestyles src="smallcaps/styles.css"/>l-DOPA can be manufactured and in its pure form is sold as a drug with the INNTooltip International Nonproprietary Name levodopa. As a drug, it is used in the treatment of Parkinson's disease and dopamine-responsive dystonia, as well as restless leg syndrome.^[5]

<templatestyles src="smallcaps/styles.css"/>l-DOPA has a counterpart with opposite chirality, <templatestyles src="smallcaps/styles.css"/>d-DOPA. As is true for many molecules, the human body produces only one of these isomers (the <templatestyles src="smallcaps/styles.css"/>l-DOPA form). The enantiomeric purity of <templatestyles src="smallcaps/styles.css"/>l-DOPA may be analyzed by determination of the optical rotation or by chiral thin-layer chromatography.^[6]

Biological role

Template:Phenylalanine biosynthesis <templatestyles src="smallcaps/styles.css"/>l-DOPA is produced from the amino acid <templatestyles src="smallcaps/styles.css"/>l-tyrosine by the enzyme tyrosine hydroxylase. <templatestyles src="smallcaps/styles.css"/>l-DOPA can act as an <templatestyles src="smallcaps/styles.css"/>l-tyrosine mimetic and be incorporated into proteins by mammalian cells in place of <templatestyles src="smallcaps/styles.css"/>l-tyrosine, generating protease-resistant and aggregate-prone proteins in vitro and may contribute to neurotoxicity with chronic <templatestyles src="smallcaps/styles.css"/>l-DOPA administration.^[7] It is also the precursor for the monoamine or catecholamine neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline). Dopamine is formed by the decarboxylation of <templatestyles src="smallcaps/styles.css"/>l-DOPA by aromatic <templatestyles src="smallcaps/styles.css"/>l-amino acid decarboxylase (AADC).

<templatestyles src="smallcaps/styles.css"/>l-DOPA can be directly metabolized by catechol-O-methyl transferase to 3-O-methyldopa, and then further to vanillactic acid. This metabolic pathway is nonexistent in the healthy body, but becomes important after peripheral <templatestyles src="smallcaps/styles.css"/>l-DOPA administration in patients with Parkinson's disease or in the rare cases of patients with AADC enzyme deficiency.^[8]

<templatestyles src="smallcaps/styles.css"/>l-Phenylalanine, <templatestyles src="smallcaps/styles.css"/>l-tyrosine, and <templatestyles src="smallcaps/styles.css"/>l-DOPA are all precursors to the biological pigment melanin. The enzyme tyrosinase catalyzes the oxidation of <templatestyles src="smallcaps/styles.css"/>l-DOPA to the reactive intermediate dopaquinone, which reacts further, eventually leading to melanin oligomers. In addition, tyrosinase can convert tyrosine directly to <templatestyles src="smallcaps/styles.css"/>l-DOPA in the presence of a reducing agent such as ascorbic acid.^[9]

Chemistry

L-DOPA, also known as L-3,4-dihydroxyphenylalanine or L-3-hydroxytyrosine, is an aromatic amino acid derived from L-phenylalanine and L-tyrosine. It is a phenethylamine, monoamine, and catecholamine, and is a biological precursor of the neurotransmitters dopamine (3,4-dihydroxyphenethylamine), norepinephrine (3,4,β-trihydroxyphenethylamine), and epinephrine (3,4,β-trihydroxy-N-methylphenethylamine).

Synthesis

File:L-dopaSyn.svg

Synthesis of <templatestyles src="smallcaps/styles.css"/>l-DOPA via hydrogenation with C₂-symmetric diphosphine.

History

<templatestyles src="smallcaps/styles.css"/>l-DOPA was first isolated from the seeds of the Vicia faba (broad bean) plant in 1913 by Swiss biochemist Markus Guggenheim.^[10]

The 2001 Nobel Prize in Chemistry was also related to <templatestyles src="smallcaps/styles.css"/>l-DOPA: the Nobel Committee awarded one-quarter of the prize to William S. Knowles for his work on chirally catalysed hydrogenation reactions, the most noted example of which was used for the synthesis of <templatestyles src="smallcaps/styles.css"/>l-DOPA.^[11]^[12]^[13]

Other organisms

Marine adhesion

<templatestyles src="smallcaps/styles.css"/>l-DOPA is a key compound in the formation of marine adhesive proteins, such as those found in mussels.^[14]^[15] It is believed to be responsible for the water-resistance and rapid curing abilities of these proteins. <templatestyles src="smallcaps/styles.css"/>l-DOPA may also be used to prevent surfaces from fouling by bonding antifouling polymers to a susceptible substrate.^[16] The versatile chemistry of <templatestyles src="smallcaps/styles.css"/>l-DOPA can be exploited in nanotechnology.^[17] For example, DOPA-containing self-assembling peptides were found to form functional nanostructures, adhesives and gels.^[18]^[19]^[20]^[21]

In plants and in the environment

In plants, L-DOPA functions as an allelochemical which inhibits the growth of certain species, and is produced and secreted by a few legume species such as the broad bean Vicia faba and the velvet bean Mucuna pruriens.^[22] Its effect is strongly dependent on the pH and the reactivity of iron in the soil.^[23] A 2025 study reported that exogenous L-DOPA triggers a rapid iron-deficiency response in plants, independent of their iron nutritional status. ^[24] L-DOPA was also suggested to protect Arabidopsis plants against cadmium toxicity. ^[25]

L-DOPA can also be found in cephalopod ink.^[26]

Use as a medication and supplement

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L-DOPA is used medically under the name levodopa in the treatment of Parkinson's disease and certain other medical conditions. It is usually used in combination with a peripherally selective aromatic L-amino acid decarboxylase (AAAD) inhibitor such as carbidopa or benserazide. These agents increase the strength and duration of levodopa. Combination formulations include levodopa/carbidopa and levodopa/benserazide, as well as levodopa/carbidopa/entacapone.

L-DOPA is found in high amounts in Mucuna pruriens (velvet bean) and is available and used over-the-counter as a supplement.

References

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@@ Line 1: / Line 1: @@
 {{Short description|Chemical compound}}
-{{Merge to|Levodopa|date=April 2025}}
 {{About|<small>L</small>-DOPA as a biological compound|its role as a medication and supplement|Levodopa}}
 {{cs1 config|name-list-style=vanc|display-authors=6}}
 {{DISPLAYTITLE:<small>L</small>-DOPA}}
 {{Use dmy dates|date=September 2024}}
 {{Chembox
 <!-- Images -->
@@ Line 14: / Line 12: @@
 | ImageFile2 = L-DOPA-from-xtal-view-2-3D-bs-17.png
 | ImageSize2 = 180px
+| ImageClass2 = bg-transparent
 | ImageCaption2 = [[Ball-and-stick model]] of the [[zwitterion]]ic form of <small>L</small>-DOPA found in the [[crystal structure]]<ref>{{ cite journal | title = Experimental and theoretical determination of electronic properties in Ldopa | vauthors = Howard ST, Hursthouse MB, Lehmann CW, Poyner EA | journal = [[Acta Crystallographica|Acta Crystallogr. B]] | volume = 51 | pages = 328–337 | year = 1995 | issue = 3 | doi = 10.1107/S0108768194011407 | bibcode = 1995AcCrB..51..328H | s2cid = 96802274 }}</ref>
 <!-- Names -->
@@ Line 53: / Line 52: @@
 '''{{sm|l}}-DOPA''', also known as '''{{sm|l}}-3,4-dihydroxyphenylalanine''' and used medically as '''levodopa''', is made and used as part of the normal [[biology]] of some plants<ref name="JAMANeuro">{{cite journal | vauthors = Cohen PA, Avula B, Katragunta K, Khan I | title = Levodopa Content of Mucuna pruriens Supplements in the NIH Dietary Supplement Label Database | journal = JAMA Neurology | volume = 79 | issue = 10 | pages = 1085–1086 | date = October 2022 | pmid = 35939305 | doi = 10.1001/jamaneurol.2022.2184 | pmc = 9361182 }}</ref> and animals, including humans. Humans, as well as a portion of the other animals that utilize {{sm|l}}-DOPA, make it via [[biosynthesis]] from the [[amino acid]] [[L-tyrosine|{{sm|l}}-tyrosine]].
-{{sm|l}}-DOPA is the [[precursor (chemistry)|precursor]] to the [[neurotransmitter]]s [[dopamine]], [[norepinephrine]] (noradrenaline), and [[epinephrine]] (adrenaline), which are collectively known as [[catecholamine]]s. Furthermore, {{sm|l}}-DOPA itself mediates [[Neurotrophic factors|neurotrophic factor]] release by the brain and [[central nervous system]].<ref>{{cite journal | vauthors = Lopez VM, Decatur CL, Stamer WD, Lynch RM, McKay BS | title = L-DOPA is an endogenous ligand for OA1 | journal = PLOS Biology | volume = 6 | issue = 9 | pages = e236 | date = September 2008 | pmid = 18828673 | pmc = 2553842 | doi = 10.1371/journal.pbio.0060236 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Hiroshima Y, Miyamoto H, Nakamura F, Masukawa D, Yamamoto T, Muraoka H, Kamiya M, Yamashita N, Suzuki T, Matsuzaki S, Endo I, Goshima Y | title = The protein Ocular albinism 1 is the orphan GPCR GPR143 and mediates depressor and bradycardic responses to DOPA in the nucleus tractus solitarii | journal = British Journal of Pharmacology | volume = 171 | issue = 2 | pages = 403–14 | date = January 2014 | pmid = 24117106 | pmc = 3904260 | doi = 10.1111/bph.12459 }}</ref> In some plant families (of the order [[Caryophyllales]]), {{sm|l}}-DOPA is the central precursor of a biosynthetic pathway that produces a class of pigments called [[betalain]]s.<ref>{{cite journal |vauthors= Polturak G, Breitel D, Grossman N, Sarrion-Perdigones A, Weithorn E, Pliner M, Orzaez D, Granell A, Rogachev I, Aharoni A |title=Elucidation of the first committed step in betalain biosynthesis enables the heterologous engineering of betalain pigments in plants |journal= New Phytol |volume=210 |issue=1 |pages= 269–283 |year=2016 |doi=10.1111/nph.13796 |doi-access=free |pmid=26683006 |bibcode=2016NewPh.210..269P |hdl=10251/87415 |hdl-access=free }}</ref>
+{{sm|l}}-DOPA is the [[precursor (chemistry)|precursor]] to the [[neurotransmitter]]s [[dopamine]], [[norepinephrine]] (noradrenaline), and [[epinephrine]] (adrenaline), which are collectively known as [[catecholamine]]s. Furthermore, {{sm|l}}-DOPA itself mediates [[Neurotrophic factors|neurotrophic factor]] release by the brain and [[central nervous system]].<ref>{{cite journal | vauthors = Lopez VM, Decatur CL, Stamer WD, Lynch RM, McKay BS | title = L-DOPA is an endogenous ligand for OA1 | journal = PLOS Biology | volume = 6 | issue = 9 | article-number = e236 | date = September 2008 | pmid = 18828673 | pmc = 2553842 | doi = 10.1371/journal.pbio.0060236 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Hiroshima Y, Miyamoto H, Nakamura F, Masukawa D, Yamamoto T, Muraoka H, Kamiya M, Yamashita N, Suzuki T, Matsuzaki S, Endo I, Goshima Y | title = The protein Ocular albinism 1 is the orphan GPCR GPR143 and mediates depressor and bradycardic responses to DOPA in the nucleus tractus solitarii | journal = British Journal of Pharmacology | volume = 171 | issue = 2 | pages = 403–14 | date = January 2014 | pmid = 24117106 | pmc = 3904260 | doi = 10.1111/bph.12459 }}</ref> In some plant families (of the order [[Caryophyllales]]), {{sm|l}}-DOPA is the central precursor of a biosynthetic pathway that produces a class of pigments called [[betalain]]s.<ref>{{cite journal |vauthors= Polturak G, Breitel D, Grossman N, Sarrion-Perdigones A, Weithorn E, Pliner M, Orzaez D, Granell A, Rogachev I, Aharoni A |title=Elucidation of the first committed step in betalain biosynthesis enables the heterologous engineering of betalain pigments in plants |journal= New Phytol |volume=210 |issue=1 |pages= 269–283 |year=2016 |doi=10.1111/nph.13796 |doi-access=free |pmid=26683006 |bibcode=2016NewPh.210..269P |hdl=10251/87415 |hdl-access=free }}</ref>
-{{sm|l}}-DOPA can be manufactured and in its pure form is sold as a [[drug]] with the {{Abbrlink|INN|International Nonproprietary Name}} ''[[levodopa]]''. As a drug, it is used in the [[therapy|treatment]] of [[Parkinson's disease]] and [[dopamine-responsive dystonia]], as well as [[restless leg syndrome]].<ref>{{cite journal |last1=Scholz |first1=Hanna |last2=Trenkwalder |first2=Claudia |last3=Kohnen |first3=Ralf |last4=Kriston |first4=Levente |last5=Riemann |first5=Dieter |last6=Hornyak |first6=Magdolna |title=Levodopa for the treatment of restless legs syndrome |journal=Cochrane Database of Systematic Reviews |date=15 February 2011 |volume=2011 |issue=5 |pages=CD005504 |doi=10.1002/14651858.CD005504.pub2 |pmid=21328278 |s2cid=196338172 |pmc=8889887 }}</ref>
+{{sm|l}}-DOPA can be manufactured and in its pure form is sold as a [[drug]] with the {{Abbrlink|INN|International Nonproprietary Name}} ''[[levodopa]]''. As a drug, it is used in the [[therapy|treatment]] of [[Parkinson's disease]] and [[dopamine-responsive dystonia]], as well as [[restless leg syndrome]].<ref>{{cite journal |last1=Scholz |first1=Hanna |last2=Trenkwalder |first2=Claudia |last3=Kohnen |first3=Ralf |last4=Kriston |first4=Levente |last5=Riemann |first5=Dieter |last6=Hornyak |first6=Magdolna |title=Levodopa for the treatment of restless legs syndrome |journal=Cochrane Database of Systematic Reviews |date=15 February 2011 |volume=2011 |issue=5 |article-number=CD005504 |doi=10.1002/14651858.CD005504.pub2 |pmid=21328278 |s2cid=196338172 |pmc=8889887 }}</ref>
 {{sm|l}}-DOPA has a counterpart with opposite [[chirality (chemistry)#By configuration: D- and L-|chirality]], [[D-DOPA|{{sm|d}}-DOPA]]. As is true for many molecules, the human body produces only one of these [[isomer]]s (the {{sm|l}}-DOPA form). The [[Enantiomer|enantiomeric purity]] of {{sm|l}}-DOPA may be analyzed by determination of the optical rotation or by chiral [[thin-layer chromatography]].<ref>{{cite journal | vauthors = Martens J, Günther K, Schickedanz M | title = Resolution of Optical Isomers by Thin-Layer Chromatography: Enantiomeric Purity of Methyldopa | journal = [[Arch. Pharm.]] | volume = 319 | issue = 6 | pages = 572–574 | date = 1986 | doi = 10.1002/ardp.19863190618 | s2cid = 97903386 }}</ref>
@@ Line 64: / Line 63: @@
 It is also the precursor for the [[monoamine]] or [[catecholamine]] neurotransmitters dopamine, norepinephrine (noradrenaline), and epinephrine (adrenaline). Dopamine is formed by the decarboxylation of {{sm|l}}-DOPA by [[aromatic L-amino acid decarboxylase|aromatic {{sm|l}}-amino acid decarboxylase]] (AADC).
-{{sm|l}}-DOPA can be directly metabolized by [[catechol-O-methyl transferase|catechol-''O''-methyl transferase]] to [[3-O-methyldopa|3-''O''-methyldopa]], and then further to [[vanillactic acid]]. This metabolic pathway is nonexistent in the healthy body, but becomes important after peripheral {{sm|l}}-DOPA administration in patients with Parkinson's disease or in the rare cases of patients with AADC enzyme deficiency.<ref name="pmid1281049">{{cite journal | vauthors = Hyland K, Clayton PT | title = Aromatic L-amino acid decarboxylase deficiency: diagnostic methodology | journal = Clinical Chemistry | volume = 38 | issue = 12 | pages = 2405–10 | date = December 1992 | pmid = 1281049 | doi =  10.1093/clinchem/38.12.2405| url = http://www.clinchem.org/cgi/reprint/38/12/2405.pdf | access-date = 16 October 2008 | archive-url = https://web.archive.org/web/20110607122144/http://www.clinchem.org/cgi/reprint/38/12/2405.pdf | archive-date = 7 June 2011 | url-status = dead | doi-access = free }}</ref>
+{{sm|l}}-DOPA can be directly metabolized by [[catechol-O-methyl transferase|catechol-''O''-methyl transferase]] to [[3-O-methyldopa|3-''O''-methyldopa]], and then further to [[vanillactic acid]]. This metabolic pathway is nonexistent in the healthy body, but becomes important after peripheral {{sm|l}}-DOPA administration in patients with Parkinson's disease or in the rare cases of patients with AADC enzyme deficiency.<ref name="pmid1281049">{{cite journal | vauthors = Hyland K, Clayton PT | title = Aromatic L-amino acid decarboxylase deficiency: diagnostic methodology | journal = Clinical Chemistry | volume = 38 | issue = 12 | pages = 2405–10 | date = December 1992 | pmid = 1281049 | doi =  10.1093/clinchem/38.12.2405| url = http://www.clinchem.org/cgi/reprint/38/12/2405.pdf | access-date = 16 October 2008 | archive-url = https://web.archive.org/web/20110607122144/http://www.clinchem.org/cgi/reprint/38/12/2405.pdf | archive-date = 7 June 2011 | doi-access = free }}</ref>
 {{sm|l}}-Phenylalanine, {{sm|l}}-tyrosine, and {{sm|l}}-DOPA are all precursors to the biological [[pigment]] [[melanin]]. The enzyme [[tyrosinase]] [[catalyst|catalyzes]] the [[oxidation]] of {{sm|l}}-DOPA to the reactive intermediate [[dopaquinone]], which reacts further, eventually leading to melanin [[oligomer]]s. In addition, [[tyrosinase]] can convert tyrosine directly to {{sm|l}}-DOPA in the presence of a reducing agent such as [[ascorbic acid]].<ref>{{cite journal | vauthors = Ito S, Kato T, Shinpo K, Fujita K | title = Oxidation of tyrosine residues in proteins by tyrosinase. Formation of protein-bonded 3,4-dihydroxyphenylalanine and 5-S-cysteinyl-3,4-dihydroxyphenylalanine | journal = The Biochemical Journal | volume = 222 | issue = 2 | pages = 407–11 | date = September 1984 | pmid = 6433900 | pmc = 1144193 | doi = 10.1042/bj2220407 }}</ref>
+==Chemistry==
+<small>L</small>-DOPA, also known as <small>L</small>-3,4-dihydroxyphenylalanine or <small>L</small>-3-hydroxytyrosine, is an [[aromatic amino acid]] derived from [[phenylalanine|<small>L</small>-phenylalanine]] and [[tyrosine|<small>L</small>-tyrosine]]. It is a [[substituted phenethylamine|phenethylamine]], [[monoamine]], and [[catecholamine]], and is a [[precursor (biochemistry)|biological precursor]] of the [[neurotransmitter]]s [[dopamine]] (3,4-dihydroxyphenethylamine), [[norepinephrine]] (3,4,β-trihydroxyphenethylamine), and [[epinephrine]] (3,4,β-trihydroxy-''N''-methylphenethylamine).
+===Synthesis===
+: [[File:L-dopaSyn.svg|class=skin-invert-image|thumb|center|550px|Synthesis of {{sm|l}}-DOPA via hydrogenation with C<sub>2</sub>-symmetric diphosphine.]]
 ==History==
 {{sm|l}}-DOPA was first isolated from the seeds of the ''[[Vicia faba]]'' (broad bean) plant in 1913 by Swiss biochemist Markus Guggenheim.<ref>{{cite journal | vauthors = Ovallath S, Sulthana B | title = Levodopa: History and Therapeutic Applications | journal = Annals of Indian Academy of Neurology | volume = 20 | issue = 3 | pages = 185–189 | date = 2017 | pmid = 28904446 | pmc = 5586109 | doi = 10.4103/aian.AIAN_241_17 | doi-access = free }}</ref>
-The 2001 [[Nobel Prize in Chemistry]] was also related to {{sm|l}}-DOPA: the Nobel Committee awarded one-quarter of the prize to [[William S. Knowles]] for his work on chirally catalysed [[hydrogenation]] reactions, the most noted example of which was used for the synthesis of {{sm|l}}-DOPA.<ref>{{cite journal | doi = 10.1021/ar00087a006 | title = Asymmetric hydrogenation | year = 1983 | vauthors = Knowles WS | journal = Accounts of Chemical Research | volume = 16 | issue = 3 | pages = 106–112}}</ref><ref>{{cite web | url = http://www.chem.wisc.edu/areas/reich/syntheses/dopa-monsanto-knowles.htm | title = Synthetic scheme for total synthesis of DOPA, L- (Monsanto) | publisher = UW Madison, Department of Chemistry | access-date = 30 September 2013}}</ref><ref>{{cite journal| vauthors = Knowles WS |title=Application of organometallic catalysis to the commercial production of L-DOPA|journal=Journal of Chemical Education|date=March 1986|volume=63|issue=3|pages=222|doi=10.1021/ed063p222|bibcode=1986JChEd..63..222K}}</ref>
+The 2001 [[Nobel Prize in Chemistry]] was also related to {{sm|l}}-DOPA: the Nobel Committee awarded one-quarter of the prize to [[William S. Knowles]] for his work on chirally catalysed [[hydrogenation]] reactions, the most noted example of which was used for the synthesis of {{sm|l}}-DOPA.<ref>{{cite journal | doi = 10.1021/ar00087a006 | title = Asymmetric hydrogenation | year = 1983 | vauthors = Knowles WS | journal = Accounts of Chemical Research | volume = 16 | issue = 3 | pages = 106–112}}</ref><ref>{{cite web | url = http://www.chem.wisc.edu/areas/reich/syntheses/dopa-monsanto-knowles.htm | title = Synthetic scheme for total synthesis of DOPA, L- (Monsanto) | publisher = UW Madison, Department of Chemistry | access-date = 30 September 2013}}</ref><ref>{{cite journal| vauthors = Knowles WS |title=Application of organometallic catalysis to the commercial production of L-DOPA|journal=Journal of Chemical Education|date=March 1986|volume=63|issue=3|page=222|doi=10.1021/ed063p222|bibcode=1986JChEd..63..222K}}</ref>
-: [[File:L-dopaSyn.svg|class=skin-invert-image|thumb|center|550px|Synthesis of {{sm|l}}-DOPA via hydrogenation with C<sub>2</sub>-symmetric diphosphine.]]
 == Other organisms ==
 === Marine adhesion ===
-{{sm|l}}-DOPA is a key [[chemical compound|compound]] in the formation of [[marine adhesive protein]]s, such as those found in [[mussel]]s.<ref>{{cite journal | vauthors = Waite JH, Andersen NH, Jewhurst S, Sun C | title=Mussel Adhesion: Finding the Tricks Worth Mimicking | journal=J Adhesion | volume=81 | year=2005 | pages=1–21 | doi=10.1080/00218460590944602 | issue=3–4 | s2cid=136967853 }}</ref><ref>{{cite web | url = https://www.sciencedaily.com/releases/2006/08/060816024159.htm | title = Study Reveals Details Of Mussels' Tenacious Bonds | publisher = Science Daily | date = 16 August 2006 | access-date = 30 September 2013}}</ref> It is believed to be responsible for the water-resistance and rapid curing abilities of these proteins. {{sm|l}}-DOPA may also be used to prevent surfaces from fouling by bonding antifouling polymers to a susceptible [[substrate (biochemistry)|substrate]].<ref>{{cite web | url = http://biomaterials.bme.northwestern.edu/mussel.asp | title = Mussel Adhesive Protein Mimetics | archive-url = https://web.archive.org/web/20060529181142/http://biomaterials.bme.northwestern.edu/mussel.asp | archive-date=29 May 2006 }}</ref> The versatile chemistry of {{sm|l}}-DOPA can be exploited in nanotechnology.<ref>{{cite journal | vauthors = Giuri D, Ravarino P, Tomasini C | title = L-Dopa in small peptides: an amazing functionality to form supramolecular materials | journal = Organic & Biomolecular Chemistry | volume = 19 | issue = 21 | pages = 4622–4636 | date = June 2021 | pmid = 33978030 | doi = 10.1039/D1OB00378J | s2cid = 234474122 | hdl = 11585/840774 | hdl-access = free }}</ref>  For example, DOPA-containing self-assembling peptides were found to form functional nanostructures, adhesives and gels.<ref>{{cite journal | vauthors = Fichman G, Adler-Abramovich L, Manohar S, Mironi-Harpaz I, Guterman T, Seliktar D, Messersmith PB, Gazit E | title = Seamless metallic coating and surface adhesion of self-assembled bioinspired nanostructures based on di-(3,4-dihydroxy-L-phenylalanine) peptide motif | journal = ACS Nano | volume = 8 | issue = 7 | pages = 7220–7228 | date = July 2014 | pmid = 24936704 | pmc = 4108209 | doi = 10.1021/nn502240r }}</ref><ref>{{cite journal | vauthors = Fichman G, Guterman T, Adler-Abramovich L, Gazit E | title = The Use of the Calcitonin Minimal Recognition Module for the Design of DOPA-Containing Fibrillar Assemblies | journal = Nanomaterials | volume = 4 | issue = 3 | pages = 726–740 | date = August 2014 | pmid = 28344244 | pmc = 5304689 | doi = 10.3390/nano4030726 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Fichman G, Andrews C, Patel NL, Schneider JP | title = Antibacterial Gel Coatings Inspired by the Cryptic Function of a Mussel Byssal Peptide | journal = Advanced Materials | volume = 33 | issue = 40 | pages = e2103677 | date = October 2021 | pmid = 34423482 | pmc = 8492546 | doi = 10.1002/adma.202103677 | bibcode = 2021AdM....3303677F }}</ref><ref>{{cite journal | vauthors = Maity S, Nir S, Zada T, Reches M | title = Self-assembly of a tripeptide into a functional coating that resists fouling | journal = Chemical Communications | volume = 50 | issue = 76 | pages = 11154–11157 | date = October 2014 | pmid = 25110984 | doi = 10.1039/C4CC03578J }}</ref>
+{{sm|l}}-DOPA is a key [[chemical compound|compound]] in the formation of [[marine adhesive protein]]s, such as those found in [[mussel]]s.<ref>{{cite journal | vauthors = Waite JH, Andersen NH, Jewhurst S, Sun C | title=Mussel Adhesion: Finding the Tricks Worth Mimicking | journal=J Adhesion | volume=81 | year=2005 | pages=1–21 | doi=10.1080/00218460590944602 | issue=3–4 | s2cid=136967853 }}</ref><ref>{{cite web | url = https://www.sciencedaily.com/releases/2006/08/060816024159.htm | title = Study Reveals Details Of Mussels' Tenacious Bonds | publisher = Science Daily | date = 16 August 2006 | access-date = 30 September 2013}}</ref> It is believed to be responsible for the water-resistance and rapid curing abilities of these proteins. {{sm|l}}-DOPA may also be used to prevent surfaces from fouling by bonding antifouling polymers to a susceptible [[substrate (biochemistry)|substrate]].<ref>{{cite web | url = http://biomaterials.bme.northwestern.edu/mussel.asp | title = Mussel Adhesive Protein Mimetics | archive-url = https://web.archive.org/web/20060529181142/http://biomaterials.bme.northwestern.edu/mussel.asp | archive-date=29 May 2006 }}</ref> The versatile chemistry of {{sm|l}}-DOPA can be exploited in nanotechnology.<ref>{{cite journal | vauthors = Giuri D, Ravarino P, Tomasini C | title = L-Dopa in small peptides: an amazing functionality to form supramolecular materials | journal = Organic & Biomolecular Chemistry | volume = 19 | issue = 21 | pages = 4622–4636 | date = June 2021 | pmid = 33978030 | doi = 10.1039/D1OB00378J | s2cid = 234474122 | hdl = 11585/840774 | hdl-access = free }}</ref>  For example, DOPA-containing self-assembling peptides were found to form functional nanostructures, adhesives and gels.<ref>{{cite journal | vauthors = Fichman G, Adler-Abramovich L, Manohar S, Mironi-Harpaz I, Guterman T, Seliktar D, Messersmith PB, Gazit E | title = Seamless metallic coating and surface adhesion of self-assembled bioinspired nanostructures based on di-(3,4-dihydroxy-L-phenylalanine) peptide motif | journal = ACS Nano | volume = 8 | issue = 7 | pages = 7220–7228 | date = July 2014 | pmid = 24936704 | pmc = 4108209 | doi = 10.1021/nn502240r | bibcode = 2014ACSNa...8.7220F }}</ref><ref>{{cite journal | vauthors = Fichman G, Guterman T, Adler-Abramovich L, Gazit E | title = The Use of the Calcitonin Minimal Recognition Module for the Design of DOPA-Containing Fibrillar Assemblies | journal = Nanomaterials | volume = 4 | issue = 3 | pages = 726–740 | date = August 2014 | pmid = 28344244 | pmc = 5304689 | doi = 10.3390/nano4030726 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Fichman G, Andrews C, Patel NL, Schneider JP | title = Antibacterial Gel Coatings Inspired by the Cryptic Function of a Mussel Byssal Peptide | journal = Advanced Materials | volume = 33 | issue = 40 | date = October 2021 | article-number = 2103677 | pmid = 34423482 | pmc = 8492546 | doi = 10.1002/adma.202103677 | bibcode = 2021AdM....3303677F }}</ref><ref>{{cite journal | vauthors = Maity S, Nir S, Zada T, Reches M | title = Self-assembly of a tripeptide into a functional coating that resists fouling | journal = Chemical Communications | volume = 50 | issue = 76 | pages = 11154–11157 | date = October 2014 | pmid = 25110984 | doi = 10.1039/C4CC03578J }}</ref>
+=== In plants and in the environment ===
+In plants, <small>L</small>-DOPA functions as an [[allelochemical]] which inhibits the growth of certain species, and is produced and secreted by a few legume species such as the broad bean ''[[Vicia faba]]'' and the velvet bean ''[[Mucuna pruriens]]''.<ref>{{cite journal | vauthors = Fujii Y, Shibuya T, Yasuda T| title = L-3,4-Dihydroxyphenylalanine as an Allelochemical Candidate from Mucuna pruriens (L.) DC. var. utilis | journal = Agricultural and Biological Chemistry | volume = 55 | issue = 2 | pages = 617–618 | date = 1991 | doi = 10.1080/00021369.1991.10870627 | doi-access = free }}</ref> Its effect is strongly dependent on the pH and the reactivity of iron in the soil.<ref>{{cite journal | vauthors = Hsieh EJ, Liao SW, Chang CY, Tseng CH, Wang SL, Grillet L| title = L-DOPA induces iron accumulation in roots of Ipomoea aquatica and Arabidopsis thaliana in a pH-dependent manner | journal = Botanical Studies | volume = 64 | issue = 24 | pages = 617–618 | date = 2023 | article-number = 24 | pmid = 37620733 | pmc = 10449704 | doi = 10.1186/s40529-023-00396-7 | doi-access = free | bibcode = 2023BotSt..64...24H }} </ref> A 2025 study reported that exogenous <small>L</small>-DOPA triggers a rapid iron-deficiency response in plants, independent of their iron nutritional status. <ref>{{cite journal | vauthors = Hsieh EJ, Rusli MH, Liao SW, Tseng CH, Chang CY, Wang SL, Yang TC, Chan YT, Shih YH, Hong CY, Grillet L| title = L-DOPA elicits iron deﬁciency response through root-to-shoot signaling and independently of the canonical regulatory pathway | journal = New Phytologist | date = 2025 | article-number = nph.70823 | doi = 10.1111/nph.70823 | pmid = 41408918 }} </ref> <small>L</small>-DOPA was also suggested to protect Arabidopsis plants against cadmium toxicity. <ref>{{cite journal | vauthors = Chang CY, Hsieh EJ, Wang SL, Grillet L| title = L-DOPA promotes cadmium tolerance and modulates iron deficiency genes in Arabidopsis thaliana | journal = Physiologia Plantarum | volume = 177 | date = 2025 | issue = 1 | article-number = e70024 | pmid = 39727040 | doi = 10.1111/ppl.70024 | bibcode = 2025PPlan.177E0024C }} </ref>
-=== Plants and in the environment ===
+<small>L</small>-DOPA can also be found in [[Cephalopod ink|cephalopod ink.]]<ref>{{Cite journal |last1=Lucero |first1=M. T. |last2=Farrington |first2=H. |last3=Gilly |first3=W. F. |date=August 1994 |title=Quantification of L-Dopa and Dopamine in Squid Ink: Implications for Chemoreception |journal=The Biological Bulletin |volume=187 |issue=1 |pages=55–63 |doi=10.2307/1542165 |jstor=1542165 |issn=1939-8697 |pmid=29281314 |bibcode=1994BiolB.187...55L }}</ref>
-In plants, <small>L</small>-DOPA functions as an [[allelochemical]] which inhibits the growth of certain species, and is produced and secreted by a few legume species such as the broad bean ''[[Vicia faba]]'' and the velvet bean ''[[Mucuna pruriens]]''.<ref>{{cite journal | vauthors = Fujii Y, Shibuya T, Yasuda T| title = L-3,4-Dihydroxyphenylalanine as an Allelochemical Candidate from Mucuna pruriens (L.) DC. var. utilis | journal = Agricultural and Biological Chemistry | volume = 55 | issue = 2 | pages = 617–618 | date = 1991 | doi = 10.1080/00021369.1991.10870627 }}</ref> Its effect is strongly dependent on the pH and the reactivity of iron in the soil.<ref>{{cite journal | vauthors = Hsieh EJ, Liao SW, Chang CY, Tseng CH, Wang SL, Grillet L| title = L-DOPA induces iron accumulation in roots of Ipomoea aquatica and Arabidopsis thaliana in a pH-dependent manner | journal = Botanical Studies | volume = 64 | issue = 24 | pages = 617–618 | date = 2023 | pmid = 37620733 | pmc = 10449704 | doi = 10.1186/s40529-023-00396-7 | doi-access = free | bibcode = 2023BotSt..64...24H }}</ref> <small>L</small>-DOPA can also be found in [[Cephalopod ink|cephalopod ink.]]<ref>{{Cite journal |last1=Lucero |first1=M. T. |last2=Farrington |first2=H. |last3=Gilly |first3=W. F. |date=August 1994 |title=Quantification of L-Dopa and Dopamine in Squid Ink: Implications for Chemoreception |url=https://pubmed.ncbi.nlm.nih.gov/29281314 |journal=The Biological Bulletin |volume=187 |issue=1 |pages=55–63 |doi=10.2307/1542165 |jstor=1542165 |issn=1939-8697 |pmid=29281314}}</ref>
 == Use as a medication and supplement ==

L-DOPA: Difference between revisions

Latest revision as of 05:06, 21 December 2025

Contents

Biological role

Chemistry

Synthesis

History

Other organisms

Marine adhesion

In plants and in the environment

Use as a medication and supplement

References

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L-DOPA: Difference between revisions

Latest revision as of 05:06, 21 December 2025

Biological role

Chemistry

Synthesis

History

Other organisms

Marine adhesion

In plants and in the environment

Use as a medication and supplement

References

Navigation menu

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