Skip to content

Study · Not a test of the peptide alone · 2023

3 results

Feasibility of Transport of 26 Biologically Active Ultrashort Peptides via LAT and PEPT Family Transporters.

Khavinson VK, Linkova NS, Rudskoy AI, Petukhov MG

Biomolecules17 Mar 2023Cited by 6 (Europe PMC)

PMID36979488 (opens in a new tab)PMCIDPMC10046148 (opens in a new tab)DOI10.3390/biom13030552 (opens in a new tab)PepBankPUB-36979488
Download PDFPubMedAsk about this study
Jump to 3 results

Summary

The aim of this work is to verify the possibility of transport of 26 biologically active ultrashort peptides (USPs) into cells via LAT and PEPT family transporters. Molecular modeling and computer-assisted docking of peptide ligands revealed that the size and structure of ligand-binding sites of the amino acid transporters LAT1, LAT2, and of the peptide transporter PEPT1 are sufficient for the transport of the 26 biologically active di-, tri-, and tetra-peptides. Comparative analysis of the binding of all possible di- and tri-peptides (8400 compounds) at the binding sites of the LAT and PEPT family transporters has been carried out. The 26 biologically active USPs systematically showed higher binding scores to LAT1, LAT2, and PEPT1, as compared with di- and tri-peptides, for which no biological activity has been established. This indicates an important possible role which LAT and PEPT family transporters may play in a variety of biological activities of the 26 biologically active peptides under investigation in this study. Most of the 26 studied USPs were found to bind to the LAT1, LAT2, and PEPT1 transporters more efficiently than the known substrates or inhibitors of these transporters. Peptides ED, DS, DR, EDR, EDG, AEDR, AEDL, KEDP, and KEDG, and peptoids DS7 and KE17 with negatively charged Asp- or Glu- amino acid residues at the N-terminus and neutral or positively charged residues at the C-terminus of the peptide are found to be the most effective ligands of the transporters under investigation. It can be assumed that the antitumor effect of the KE, EW, EDG, and AEDG peptides could be associated with their ability to inhibit the LAT1, LAT2, and PEPT1 amino acid transporters. The data obtained lead to new prospects for further study of the mechanisms of transport of USP-based drugs into the cell and design of new antitumor drugs.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study3

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone3

In this study, the peptide was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking the peptide.

  1. 01Computer modelNot a test of Epitalon aloneIn silicoActivity measurement

    In docking models, the 26 biologically active ultrashort peptides, a pool that includes AEDG, had higher binding scores to LAT1, LAT2 and PEPT1 than peptides without known activity.

    In plain wordsIn computer models, a group of 26 short peptides, including AEDG, bound the transporters better than inactive peptides.

    Peptide
    Epitalon
    Outcome
    IncreaseBinding score to LAT1, LAT2 and PEPT1 versus peptides without known activity
    Study

    n: not reported in source

    Molecular docking to LAT1, LAT2 and PEPT1
    Comparator
    Di- and tri-peptides with no established biological activity
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    The 26 biologically active USPs systematically showed higher binding scores to LAT1, LAT2, and PEPT1, as compared with di- and tri-peptides, for which no biological activity has been established.
    2 context sentences
    Summary · context
    It can be assumed that the antitumor effect of the KE, EW, EDG, and AEDG peptides could be associated with their ability to inhibit the LAT1, LAT2, and PEPT1 amino acid transporters.
    Summary · context
    The aim of this work is to verify the possibility of transport of 26 biologically active ultrashort peptides (USPs) into cells via LAT and PEPT family transporters.

    In this study, Epitalon was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Epitalon.

  2. 02Computer modelNot a test of Epitalon aloneIn silicoActivity measurement

    In docking models, most of the 26 ultrashort peptides, a pool that includes AEDG, bound LAT1, LAT2 and PEPT1 more efficiently than known substrates or inhibitors.

    In plain wordsIn computer models, most of 26 short peptides, including AEDG, bound the transporters better than known substrates or inhibitors.

    Peptide
    Epitalon
    Outcome
    IncreaseBinding to LAT1, LAT2 and PEPT1 versus known substrates or inhibitors
    Study

    n: not reported in source

    Molecular docking to LAT1, LAT2 and PEPT1
    Comparator
    Known substrates or inhibitors of the transporters
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Most of the 26 studied USPs were found to bind to the LAT1, LAT2, and PEPT1 transporters more efficiently than the known substrates or inhibitors of these transporters.
    2 context sentences
    Summary · context
    It can be assumed that the antitumor effect of the KE, EW, EDG, and AEDG peptides could be associated with their ability to inhibit the LAT1, LAT2, and PEPT1 amino acid transporters.
    Summary · context
    The aim of this work is to verify the possibility of transport of 26 biologically active ultrashort peptides (USPs) into cells via LAT and PEPT family transporters.

    In this study, Epitalon was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Epitalon.

  3. 03Computer modelNot a test of Chonluten (EDG) aloneIn silicoMechanism

    Docking analyses identified EDG among the most effective ligands of the investigated transporters.

    In plain wordsComputer analyses identified EDG among the most effective ligands of the studied transporters.

    Peptide
    Chonluten (EDG)
    Outcome
    Not applicablePredicted transporter ligand ranking
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Peptides ED, DS, DR, EDR, EDG, AEDR, AEDL, KEDP, and KEDG, and peptoids DS7 and KE17 with negatively charged Asp- or Glu- amino acid residues at the N-terminus and neutral or positively charged residues at the C-terminus of the peptide are found to be the most effective ligands of the transporters under investigation.
    1 context sentence
    Summary · context
    The aim of this work is to verify the possibility of transport of 26 biologically active ultrashort peptides (USPs) into cells via LAT and PEPT family transporters.

    In this study, Chonluten (EDG) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Chonluten (EDG).

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Versions 4 to 10Current

    28 Oct 2026, 02:02 UTC

    The same notice was added 7 times, first on 21 Oct 2026, 17:05 UTC. The status did not change between them.

    Study results updated

  2. Version 3

    21 Oct 2026, 16:35 UTC

    Study data updated · source update from Europe PMC

  3. Version 2

    10 Oct 2026, 08:19 UTC

    Study results updated

  4. Version 1

    9 Oct 2026, 02:47 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

PepBank is a research reference. Talk to a doctor before you use any peptide.