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

Mechanism / theoretical grounding — not clinical validation.

Khavinson VK, Linkova NS, Rudskoy AI, Petukhov MG. Biomolecules. 2023.

Organ: general-aging · Type: theoretical · Peptides: Vilon, Epitalon, Testagen, Pinealon, Bronchogen

Open-access in-silico docking of 26 ultrashort peptides, including KEDG, into LAT1, LAT2, and PEPT1 — computational transport feasibility only, not cellular uptake data and not a fertility study.

Editorial summary of a 2023 Biomolecules article (MDPI, open access: doi:10.3390/biom13030552). Docking of ultrashort peptides into amino-acid and peptide transporters. Public pages cite PubMed; the DOI is the OA record. Read the paper: PMID 36979488.

Methods

Molecular modeling and computer-assisted docking of 26 biologically active di-, tri-, and tetrapeptides into ligand-binding sites of LAT1, LAT2, and PEPT1, with a comparative screen of all possible di- and tripeptides (8400 compounds). The authors also compare scores with known substrates or inhibitors of those transporters. No wet-lab uptake assay is described in the abstract.

Findings

Binding-site size was judged sufficient for the 26 peptides. Those 26 systematically scored higher than di- and tripeptides without established biological activity in this library. Most of the 26 bound more efficiently in the model than known substrates or inhibitors. Peptides with N-terminal Asp or Glu and a neutral or positive C-terminus (including ED, DS, DR, EDR, EDG, AEDR, AEDL, KEDP, and KEDG, and peptoids DS7 and KE17) ranked as the most effective ligands. The authors speculate that antitumor reports for KE, EW, EDG, and AEDG could relate to LAT/PEPT inhibition.

KEDG appears here only as an in-silico LAT/PEPT ligand. This is not evidence of Testagen uptake in gonad tissue and not a clinical result. Follow the PMID and the OA DOI.