Semax · research summary

Semax, a Copper Chelator Peptide, Decreases the Cu(II)-Catalyzed ROS Production and Cytotoxicity of aβ by Metal Ion Stripping and Redox Silencing.

Bioinorganic chemistry and applications · 2025. Summary drawn from the study's full text. Each statement is followed by the exact sentence it comes from. This is a research summary, not medical advice.

Study type

In vitro and in-cell experiments investigating the inhibition of copper-catalyzed oxidation of amyloid-β by Semax.
“The ability of the peptide Semax to inhibit the copper-catalyzed oxidation of aβ was studied in vitro and discussed.”

Subjects

Amyloid-β peptides (aβ1–16, aβ1–28, aβ1–40), copper ions, ascorbate, and human neuroblastoma SH-SY5Y cells.
“We employed aβ1–16 and aβ1–28 as well-established model peptides for our in vitro studies since they contain all the copper binding residues and do not readily precipitate or aggregate in the experimental condition used.”

Sample size

Three independent experiments performed in triplicate for UV and fluorescence measurements; 20,000 cells analyzed per sample for flow cytometry.
“Results of all UV measurements are the average of three independent experiments.”

Duration

In vitro reactions monitored over 30 minutes; cell treatments lasted 24 hours.
“Following 24 h of treatments, SH-SY5Y cell viability was estimated by using the MTT assay (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide) as described previously [100].”

Reported findings

Semax extracts Cu(II) from Cu(II)-aβ complexes and influences the redox cycling to decrease ROS production.
“The results indicate that Semax is able to extract Cu(II) from Cu(II)-aβ species as well as to influence the redox cycling of the Cu(II)-aβ complex and decrease the level of associated ROS production.”
Semax reduces the percentage of cells with increased ROS levels when exposed to Cu(II) and ascorbate with or without aβ.
“The presence of stoichiometric amounts of Semax significantly decreases the percentage of DCF positive cells, both in absence (Figure 4(b), red curve) or in presence of aβ (Figure 4(c), red curve) with a percentage of 41% and 40% of cells in the M1 region, respectively.”
Semax lowers the cytotoxic effect of Cu(II) plus ascorbate and Cu(II) plus ascorbate plus aβ on SH-SY5Y cells.
“As expected, the presence of Semax significantly lowered the cytotoxic effect of Cu(II) + ascorbate and Cu(II) + ascorbate + aβ (viability of 83% and 82%, respectively), which is consistent with all the other data showed.”

Source: PubMed 40496623 · DOI 10.1155/bca/4226220 · all study summaries

Subjects

Amyloid-β peptides (aβ1–16, aβ1–28, aβ1–40), copper ions, ascorbate, and human neuroblastoma SH-SY5Y cells.

“We employed aβ1–16 and aβ1–28 as well-established model peptides for our in vitro studies since they contain all the copper binding residues and do not readily precipitate or aggregate in the experimental condition used.”

Reported findings

Semax extracts Cu(II) from Cu(II)-aβ complexes and influences the redox cycling to decrease ROS production.

“The results indicate that Semax is able to extract Cu(II) from Cu(II)-aβ species as well as to influence the redox cycling of the Cu(II)-aβ complex and decrease the level of associated ROS production.”

Semax reduces the percentage of cells with increased ROS levels when exposed to Cu(II) and ascorbate with or without aβ.

“The presence of stoichiometric amounts of Semax significantly decreases the percentage of DCF positive cells, both in absence (Figure 4(b), red curve) or in presence of aβ (Figure 4(c), red curve) with a percentage of 41% and 40% of cells in the M1 region, respectively.”

Semax lowers the cytotoxic effect of Cu(II) plus ascorbate and Cu(II) plus ascorbate plus aβ on SH-SY5Y cells.

“As expected, the presence of Semax significantly lowered the cytotoxic effect of Cu(II) + ascorbate and Cu(II) + ascorbate + aβ (viability of 83% and 82%, respectively), which is consistent with all the other data showed.”