# 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.

> PubMed lists PMID 27586814 in Journal of inorganic biochemistry as Journal Article, Research Support, Non-U.S. Gov't, with publication-date metadata of 2016-08-27 (day precision). PeptideScanner associated the retained record with the identity slug semax. These fields reproduce attributed bibliographic metadata and do not summarize or endorse the article's findings.

- Evidence object: `story:pubmed-pmid-27586814-semax:v1`
- Evidence domain: Literature metadata
- Date in source: 2018-03-12
- Source checked: 2026-07-30
- Published by PeptideScanner: 2026-08-13
- Story landing page: https://peptidescanner.com/stories/pubmed-pmid-27586814-semax/
- JSON record: https://peptidescanner.com/evidence/v1/objects/pubmed-pmid-27586814-semax-v1.json
- Content SHA-256: `a2cdcf37fa14a7d5b225a24901117347ed38c26f261858dab36980a46a80ace6`

## Claims and source pins

### Headline

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. ([`pubmed-observation-pmid-27586814-2018-03-12-c9cdf57a5b6b`](#source-pubmed-observation-pmid-27586814-2018-03-12-c9cdf57a5b6b))

### Summary

PubMed lists PMID 27586814 in Journal of inorganic biochemistry as Journal Article, Research Support, Non-U.S. Gov't, with publication-date metadata of 2016-08-27 (day precision). PeptideScanner associated the retained record with the identity slug semax. These fields reproduce attributed bibliographic metadata and do not summarize or endorse the article's findings. ([`pubmed-observation-pmid-27586814-2018-03-12-c9cdf57a5b6b`](#source-pubmed-observation-pmid-27586814-2018-03-12-c9cdf57a5b6b))

### Paragraph 1

PubMed lists PMID 27586814 in Journal of inorganic biochemistry as Journal Article, Research Support, Non-U.S. Gov't, with publication-date metadata of 2016-08-27 (day precision). PeptideScanner associated the retained record with the identity slug semax. These fields reproduce attributed bibliographic metadata and do not summarize or endorse the article's findings. ([`pubmed-observation-pmid-27586814-2018-03-12-c9cdf57a5b6b`](#source-pubmed-observation-pmid-27586814-2018-03-12-c9cdf57a5b6b))

### Paragraph 2

This page reproduces bounded bibliographic metadata attributed to PubMed. Its title and publication details are source metadata, not PeptideScanner's endorsement or an assertion of safety, efficacy, or scientific truth. ([`pubmed-observation-pmid-27586814-2018-03-12-c9cdf57a5b6b`](#source-pubmed-observation-pmid-27586814-2018-03-12-c9cdf57a5b6b))

## Sources

<a id="source-pubmed-observation-pmid-27586814-2018-03-12-c9cdf57a5b6b"></a>
- **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. · retained source version 1:2018-03-12:current:c9cdf57a5b6bd3ad40059382d556a26ed427133b6a67a8358edd55e1a5c25990** — PubMed; class A. [Open source](https://pubmed.ncbi.nlm.nih.gov/27586814/) (`pubmed-observation-pmid-27586814-2018-03-12-c9cdf57a5b6b`)

## Correction lineage

No correction is recorded for this version.

## Reporting boundaries and unknowns

PeptideScanner reproduces bounded bibliographic metadata attributed to PubMed. It does not summarize or endorse the article's findings.

- Sources outside the selected public PeptideScanner bundle may exist and are not represented by this object.
- This object does not determine whether cited records agree, corroborate one another, or establish scientific truth.
- This object does not determine safety, efficacy, causality, or suitability for any person.

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## Suggested citation

PeptideScanner. "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." Version 1, published 2026-08-13. https://peptidescanner.com/evidence/v1/objects/pubmed-pmid-27586814-semax-v1.json SHA-256: a2cdcf37fa14a7d5b225a24901117347ed38c26f261858dab36980a46a80ace6.

