Rubiscolin

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The rubiscolins are a group of opioid peptides that are formed during digestion of the ribulose bisphosphate carboxylase/oxygenase (Rubisco) protein from spinach leaves. Two of them are known, [1] acting as weak agonists of the delta opioid receptor selective for the G protein signaling pathway. [2]

Contents

Background

Rubisco is a key protein in carbon fixation and is found in photosynthetic organs such as leaves in very high concentration. It usually accounts for 40% of the protein mass of a plant. [3] With all forms of RuBisCO (not only plants, but also bacteria) taken into account, RuBisCO is possibly the most abundant type of protein on Earth. [4]

The production of similar peptides from digestion of other species' Rubisco has not yet been reported.

Overview

Studies have been conducted on rubiscolin structure and biological responses following its digestion. [5] [6] The tertiary structure and biological function of spinach-derived rubiscolin has been analyzed in the laboratory. [5]

When rubiscolin is digested, studies have shown that rubiscolin has the potential to bind to δ opioid receptors in the body. [5] The analysis of the amino acids responsible for this agonistic relationship of rubiscolin with δ opioid receptors can lead to replication of these proteins in the lab. [5] Rubiscolin has the capability to bind to δ opioid receptors following its digestion. [5] Rubiscolin-5 and -6 are unusual delta opioid receptor agnoists in that they mainly activate the G protein signaling pathway at the receptor, mostly leaving the β-arresting pathway alone. [2]

Types of rubiscolin

Several peptides are known to be produced after digestion of rubiscolin in various ways.

Rubiscolin-5

Rubiscolin-6

Other bioactive Rubisco-derived peptides

MRW

MRWRD

IAYKPAG

LRIPVA

References

  1. ↑ Yang, Shuzhang; Yunden, Jinsmaa; Sonoda, Soushi; Doyama, Naomi; Lipkowski, Andrzej W; Kawamura, Yukio; Yoshikawa, Masaaki (2001). "Rubiscolin, a δ selective opioid peptide derived from plant Rubisco". FEBS Letters. 509 (2): 213–217. doi:10.1016/S0014-5793(01)03042-3. PMID   11741591. S2CID   83631217.
  2. 1 2 Cassell, Robert J.; Mores, Kendall L.; Zerfas, Breanna L.; Mahmoud, Amr H.; Lill, Markus A.; Trader, Darci J.; van Rijn, Richard M. (March 2019). "Rubiscolins are naturally occurring G protein-biased delta opioid receptor peptides". European Neuropsychopharmacology. 29 (3): 450–456. doi:10.1016/j.euroneuro.2018.12.013.
  3. ↑ Heazlewood J (2012). Proteomic applications in biology. New York: InTech Manhattan. ISBN   978-953-307-613-3.
  4. ↑ Cooper GM (2000). "10.The Chloroplast Genome". The Cell: A Molecular Approach (2nd ed.). Washington, D.C.: ASM Press. ISBN   978-0-87893-106-4. , one of the subunits of ribulose bisphosphate carboxylase (rubisco) is encoded by chloroplast DNA. Rubisco is the critical enzyme that catalyzes the addition of CO2 to ribulose-1,5-bisphosphate during the Calvin cycle. It is also thought to be the single most abundant protein on Earth, so it is noteworthy that one of its subunits is encoded by the chloroplast genome.
  5. 1 2 3 4 5 Caballero, Julio; Saavedra, Mario; Fernández, Michael; González-Nilo, Fernando D. (2007-10-01). "Quantitative Structure–Activity Relationship of Rubiscolin Analogues as δ Opioid Peptides Using Comparative Molecular Field Analysis (CoMFA) and Comparative Molecular Similarity Indices Analysis (CoMSIA)". Journal of Agricultural and Food Chemistry. 55 (20): 8101–8104. doi:10.1021/jf071031h. ISSN   0021-8561. PMID   17803260.
  6. 1 2 3 4 5 Yang, Yanjun; Marczak, Ewa D.; Yokoo, Megumi; Usui, Hachiro; Yoshikawa, Masaaki (2003-08-01). "Isolation and Antihypertensive Effect of angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides from Spinach Rubisco". Journal of Agricultural and Food Chemistry. 51 (17): 4897–4902. doi:10.1021/jf026186y. ISSN   0021-8561. PMID   12903942.
  7. ↑ Hirata, H; Sonoda, S; Agui, S; Yoshida, M; Ohinata, K; Yoshikawa, M (2007). "Rubiscolin-6, a delta opioid peptide derived from spinach Rubisco, has anxiolytic effect via activating sigma1 and dopamine D1 receptors". Peptides. 28 (10): 1998–2003. doi:10.1016/j.peptides.2007.07.024. PMID   17766012. S2CID   54430089.


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