Influence of the N-terminus acetylation of Semax, a synthetic analog of ACTH(4-10), on copper(II) and zinc(II) coordination and biological properties.

Magrì A, Tabbì G, Giuffrida A, Pappalardo G, Satriano C, Naletova I, Nicoletti VG, Attanasio F

Journal of inorganic biochemistry27 Aug 2016Cited by 7 (Europe PMC)

PMID27586814DOI10.1016/j.jinorgbio.2016.08.013PepBankPUB-27586814

Publisher page PubMedAsk about this study

Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study6

2 results from studies that gave the peptide. No result from this study comes from people.

01LabIn vitro (cell-free)Mechanism
In cell-free chemistry, the copper(II) complex of Semax with a free amino terminus was redox-stable and did not react with ascorbic acid, unlike the acetylated form.
In plain wordsIn lab tests, the copper complex of regular Semax stayed stable and did not react with ascorbic acid, unlike the acetylated form.
Peptide
Semax
Outcome
Not applicableRedox stability of Cu(II)-Semax complex
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Studied dose
Dose not stated
Source sentences
Summary
In the amino-free form, the resulting complex species is redox-stable and unreactive against ascorbic acid, unlike the acetylated form.
Report a problemFND-2758681401
02LabIn vitro (cell-free)Mechanism
In cell-free chemistry, Semax and Ac-Semax formed zinc(II) complex species with comparable strength.
In plain wordsIn lab tests, Semax and acetylated Semax formed zinc complexes with similar strength.
Peptide
Semax
Outcome
Not applicableZn(II) complex formation by Semax
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Studied dose
Dose not stated
Source sentences
Summary
Both peptides were able to form Zn(II) complex species with comparable strength.
Report a problemFND-2758681402

Studies that did not test the peptide alone4

In this study, Semax 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 Semax.

03LabNot a test of Semax aloneIn vitro (cells)Activity measurement
In SH-SY5Y neuroblastoma cells, acetylated Semax did not protect against Cu(II)-induced toxicity.
In plain wordsIn cells, acetylated Semax did not protect against copper-induced toxicity.
Peptide
Semax
Outcome
No significant changeProtection from Cu(II)-induced toxicity by Ac-Semax
Study
n: not reported in source
SH-SY5Y neuroblastoma cell line
Outcome group
Neuroprotection · Nervous system and cognition
Source sentences
Summary
Semax acetylation did not protect from Cu(II) induced toxicity on a SH-SY5Y neuroblastoma cell line, thus demonstrating the crucial role played by the free NH₂ terminus in the cell protection.
In this study, Semax 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 Semax.
Report a problemFND-2758681404
04LabNot a test of Semax aloneIn vitro (cells)Mechanism
In neuroblastoma cells, acetylation of the peptide amino group did not change Zn(II) influx.
In plain wordsIn cells, acetylating the peptide did not change how much zinc entered the cells.
Peptide
Semax
Outcome
No significant changeZn(II) influx after peptide acetylation
Study
n: not reported in source
neuroblastoma cells
Outcome group
Receptor activity and mechanism · Nervous system and cognition
Source sentences
Summary
Confocal microscopy imaging confirmed that peptide group acetylation does not affect the Zn(II) influx in neuroblastoma cells.
In this study, Semax 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 Semax.
Report a problemFND-2758681405
05LabNot a test of Semax aloneIn vitro (cell-free)Mechanism
In cell-free chemistry, the main copper(II) complex of acetylated Semax had a more positive formal redox potential than the corresponding Cu(II)-Semax species.
In plain wordsIn lab tests, the copper complex of acetylated Semax had a more positive redox potential than the copper complex of Semax.
Peptide
Semax
Outcome
Not applicableRedox potential of Cu(II)-Ac-Semax complex
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
The reduced ligand field affects the [CuLH_-2]^2- formal redox potential, which is more positive than that of Cu(II)-Semax corresponding species.
In this study, Semax 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 Semax.
Report a problemFND-2758681403
06LabNot a test of Semax aloneIn vitro (cell-free)Mechanism
In cell-free chemistry, at physiological pH the main copper(II) complex of acetylated Semax had a distorted chromophore with a weak apical interaction of the methionine sulphur, and differed from the Cu(II)-Semax complex.
In plain wordsIn lab tests, the main copper complex of acetylated Semax had a different structure from the copper complex of Semax.
Peptide
Semax
Outcome
Not applicableCu(II) coordination of acetylated Semax at physiological pH
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
At physiological pH, the main complex species formed by Ac-Semax, [CuLH_-2]^2-, consists in a distorted CuN₃O chromophore with a weak apical interaction of the methionine sulphur.
In this study, Semax 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 Semax.
Report a problemFND-2758681406

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.

Version 2Current
10 Oct 2026, 10:21 UTC
Study results updated
Version 1
9 Oct 2026, 03:04 UTC
First added · source update from Europe PMC

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