The antimicrobial and anti-endotoxic peptide AmyI-1-18 from rice α-amylase and its [N3L] analog promote angiogenesis and cell migration.
Taniguchi. Masayuki M; Ochiai. Akihito A; Namae. Toshiki T; Saito. Kazuki K; Kato. Tetsuo T; Saitoh. Eiichi E; Tanaka. Takaaki T
Key Findings
- Both AmyI-1-18 and its [N3L] analog boost proliferation of HUVEC cells in a dose‑dependent way.
- At 1 µM they promote tube formation (a model of angiogenesis) comparable to LL‑37.
- In scratch‑wound assays they enhance cell migration, with optimal concentrations of 10 µM (AmyI-1-18), 1 µM ([N3L]AmyI-1-18), and 0.1 µM (LL‑37).
- The angiogenic effect depends on VEGF receptor activation, and the [N3L] analog still works even when cell division is blocked.
Practical Outcomes
- For now, the peptides are interesting candidates for future wound‑healing or tissue‑repair supplements, but there’s no human data yet. Biohackers should wait for animal or clinical studies before trying them, and any dosing would be purely speculative at this stage.
Summary
A short peptide from rice (AmyI-1-18) and a tweaked version called [N3L]AmyI-1-18 can make human blood‑vessel cells grow, form new blood‑vessel‑like structures, and move faster in lab dishes, similar to the human peptide LL‑37. This suggests they might help heal wounds, but the work is still only in cell cultures.
Abstract
In our previous studies, we showed that AmyI-1-18 and its single amino acid-substituted analogs have antimicrobial, anti-inflammatory, and anti-endotoxic activities and cause little or no hemolysis or cytotoxicity. In this study, we investigated the potential of these peptides to promote proliferation, angiogenesis (tube formation), and migration in human umbilical vein endothelial cells (HUVECs). Among five single amino acid-substituted analogs, [N3L]AmyI-1-18 induced cell proliferation in a concentration-dependent manner with similar efficacy to AmyI-1-18. In tube formation assays, AmyI-1-18 and [N3L]AmyI-1-18 had angiogenic activities at 1 μM and their effects were similar to those of LL-37. Moreover, scratch migration assays showed that AmyI-1-18, [N3L]AmyI-1-18, and LL-37 promote cell migration with optimum concentrations of 10, 1, and 0.1 μM, respectively. Subsequently, we performed tube formation assays using HUVECs pretreated with SU5416, which is an inhibitor of vascular endothelial growth factor (VEGF) receptors, and revealed that AmyI-1-18 and [N3L]AmyI-1-18 induce angiogenesis by activating VEGF receptors. Similarly, after pretreating HUVECs with mitomycin C, which inhibits cell proliferation, [N3L]AmyI-1-18 significantly contributed to wound closure in scratch migration assays. Moreover, enhancements of hydrophobicity following substitution of AmyI-1-18 asparagine with leucine led to greater increases in cell migration. The present data indicate that both peptides, particularly [N3L]AmyI-1-18, are candidates for use as wound healing agents.
Study Information
pubmed
2018
2018-04-27T00:00:00.000Z
10.1016/j.peptides.2018.04.017
16
39