Vesilute

Also known as: Vesilut, Везилют, Glu-Asp, ED dipeptide, L-Glutamyl-L-aspartic acid, Bladder bioregulator peptide

Not FDA Approved

Not an approved medicine (US/EU); sold as a bioregulator supplement or research peptide

6 references

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TLDR

Vesilute is the synthetic dipeptide Glu-Asp (ED), listed by Khavinson's institute as a "bladder regulator" bioregulator peptide. Apart from computer-modeling papers that include it among dozens of short peptides, no human, animal or cell studies of Vesilute appear in PubMed. Its claimed urinary benefits are unproven.

At a Glance

Classification: Synthetic dipeptide (L-glutamyl-L-aspartate); Khavinson-school "ultrashort" peptide bioregulator; marketed as a urinary-system (bladder) regulator

Vesilute is a two-amino-acid peptide, glutamic acid bonded to aspartic acid (Glu-Asp, or "ED"). It belongs to the family of short "peptide bioregulators" developed by Vladimir Khavinson's St. Petersburg Institute of Bioregulation and Gerontology. That family also includes Vilon (Lys-Glu), Vesugen (Lys-Glu-Asp), Livagen and Epitalon. In that group's papers, ED is listed as a "bladder regulator" or "genitourinary system regulator". It is sold mainly as a dietary-supplement-style bioregulator in Russia and by online vendors. What Vesilute is studied for: • Bladder and urinary function, as claimed by the developers • Computer modeling of how short peptides enter cells through amino acid and peptide transporters. Important: we found no published primary studies (human, animal or cell) testing Vesilute itself in PubMed. It appears only in tables and lists within the developing group's review and modeling papers. Its "bladder regulator" label is not backed by indexed experimental data. Vesilute is not an approved medicine in the US, EU or, as far as we can tell, as a registered drug in Russia.

What Is Vesilute?

Vesilute is a defined synthetic dipeptide: L-Glutamic acid — L-Aspartic acid (Glu-Asp, ED) Molecular weight: about 262 g/mol (PubChem CID 99716 for Glu-Asp). It is the smallest member of a group of related Khavinson peptides that share an "ED" (Glu-Asp) motif, including Vesugen (KED), Pinealon (EDR), Chonluten (EDG) and Epitalon (AEDG). Product labelling caution: some vendors list Vesilute with the Lys-Glu-Asp sequence, which actually belongs to Vesugen, and at least one older abstract printed the sequence as Gly-Asp. In the developers' own recent papers, Vesilut is ED (Glu-Asp).

What Are Researchers Studying?

Cell entry of short peptides (computer modeling)

The Khavinson group used molecular docking to predict whether 20+ short bioregulator peptides could be carried into cells by amino acid (LAT) and peptide (PEPT) transporters. ED ranked among the strongest predicted binders to LAT1 and LAT2. The authors suggest that high LAT1 levels in the kidney and bladder could help explain tissue-specific effects.

Bladder and urinary function (claimed)

The developers classify ED as a urinary-system regulator, but we found no indexed experimental or clinical studies of ED on bladder function. Separate Russian studies tested a bladder-tissue peptide extract in older adults with bladder symptoms. That extract is a different product, not the synthetic ED dipeptide (see notes).

How Does It Work?

No mechanism has been shown experimentally for Vesilute. The developing group's general hypothesis for its short peptides: Short peptide ↓ enters cells through amino acid or peptide transporters (LAT1, LAT2, PEPT1/2), as predicted by computer modeling ↓ reaches the nucleus and binds specific DNA sequences or histone proteins ↓ adjusts expression of tissue-specific genes ("tissue-specific bioregulation"). For ED specifically, computer docking studies predicted strong binding to the LAT1 and LAT2 transporters, among the strongest of the peptides modeled. These are computer predictions, not lab measurements, and the gene-regulation theory has seen little independent testing.

What Does the Research Show?

Human research

NONE IDENTIFIED No human studies of Vesilute were found in PubMed.

Animal research

NONE IDENTIFIED

In-vitro research

VERY LOW Only computer (in silico) docking studies that include ED among many peptides.

What We Still Don't Know

• Whether Vesilute has any effect on the bladder or urinary system in cells, animals or people • Whether it reaches tissues intact; dipeptides are normally broken down quickly into amino acids • Whether the transporter-binding predictions hold up in lab experiments • Whether the proposed DNA- or histone-binding mechanism is real for ED • Safety, including in long-term use • What vendor products actually contain, given sequence mix-ups with Vesugen (KED). Evidence for Vesilute is essentially absent beyond the developers' classification and computer modeling.

Related Compounds

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Sources & References

  1. Khavinson V, Linkova N, Kozhevnikova E, et al. Transport of Biologically Active Ultrashort Peptides Using POT and LAT Carriers. Int J Mol Sci. 2022;23(14). (Lists "Vesilut (ED)" as a bladder regulator; in silico docking.)
  2. Khavinson VK, Linkova NS, Rudskoy AI, Petukhov MG. Feasibility of Transport of 26 Biologically Active Ultrashort Peptides via LAT and PEPT Family Transporters. Biomolecules. 2023;13(3). (ED included; in silico docking.)
  3. Khavinson VK, Popovich IG, Linkova NS, et al. Peptide Regulation of Gene Expression: A Systematic Review. Molecules. 2021;26(22). (Background on the group's gene-regulation hypothesis; not specific to ED.)
  4. Gomberg VG, Ryzhak AP, Lyutov RV. [Correction of age related bladder function decrease with peptide geroprotector in women]. Adv Gerontol. 2013;26(2):309–314. (Russian; bladder-tissue peptide extract, NOT Vesilute.)
  5. Gomberg VG, Ryzhak VG, Liutov RV. [Peptide geroprotector application for treatment of elderly and senile patients with prostatic hyperplasia]. Adv Gerontol. 2013;26(3):476–480. (Russian; bladder-tissue peptide extract, NOT Vesilute.)
  6. PubChem. Glu-Asp (CID 99716).

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