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N-Acetyl Selank Amidate Research Reference

Selank with N-terminal acetyl and C-terminal amide caps · Terminal-capping and peptidase-stability research

Classification

TYPE

Synthetic heptapeptide, N-acetylated and C-amidated

Domain

Neurochemical Research Peptides

Format

Lyophilized reference compound

Quick Specs

Molecular Weight

792.9 g/mol

Purity

≥98% (HPLC)

Storage

−20 °C, desiccated

Appearance

White lyophilized powder

Solubility

Soluble in water

01

Research Overview

N-Acetyl Selank Amidate is Selank (Thr-Lys-Pro-Arg-Pro-Gly-Pro) with both ends capped: an acetyl group on the N-terminus and an amide on the C-terminus. Capping both termini is a common strategy for making short peptides more resistant to exopeptidases, the enzymes that trim peptides from their ends.

The core sequence, and therefore its relationship to tuftsin and Selank, is unchanged. It is supplied as a lyophilized reference material for in vitro research, particularly for comparing capped and uncapped versions of the same peptide.

02

Structural & Sequence Context

The peptide keeps Selank’s seven residues and modifies only the ends.

Core sequence
Thr-Lys-Pro-Arg-Pro-Gly-Pro: the tuftsin tetrapeptide followed by the stabilising Pro-Gly-Pro tail.

N-terminal acetyl group
Replaces the free N-terminal amine with an acetamide. This blocks aminopeptidases, removes one positive charge and adds 42 Da.

C-terminal amide
Replaces the free C-terminal carboxylate with a carboxamide. This blocks carboxypeptidases, removes one negative charge and lowers the mass by about 1 Da.

Net effect
Compared with Selank, the molecule is about 41 Da heavier, has no free terminal amine or carboxylate, and keeps the positive charges of Lys2 and Arg4.

03

Mechanistic Research Context

Research interest in the capped form is mainly comparative.

Exopeptidase resistance
Blocking both termini is expected to slow breakdown by aminopeptidases and carboxypeptidases, which can be measured in serum or tissue homogenate incubations against unmodified Selank.

Relation to Selank research
Its biological activity is generally assumed to follow that of Selank, but direct published data on the capped form are limited. Side-by-side testing is the most reliable way to compare them.

Charge and permeability
Removing the terminal charges changes polarity, which may affect membrane interactions and chromatographic behaviour.

These points are research context only; no effects are claimed for this material.

04

Laboratory Applications

Capped versus uncapped comparisons
Paired with Selank to measure how terminal capping affects stability, retention and activity in vitro.

Peptidase studies
A substrate for testing endopeptidase activity when exopeptidase routes are blocked.

Analytical reference
Useful for developing methods that distinguish closely related capped and uncapped peptides.

05

Stability & Handling

Storage
Store the lyophilized powder at −20 °C, sealed and desiccated.

Reconstitution
Soluble in water and aqueous buffers thanks to its lysine and arginine residues.

Enzymatic breakdown
Terminal capping slows but does not stop degradation; internal bonds can still be cleaved by endopeptidases.

Solutions
Prepare fresh or freeze single-use aliquots, and use low-binding polypropylene tubes.

06

Analytical & Purity Considerations

Analysis must confirm both terminal modifications.

HPLC
Reversed-phase C18 with a TFA gradient. With its terminal charges removed, it usually retains slightly longer than Selank under the same conditions. Detect at about 214 nm.

Mass spectrometry
Positive-mode ESI shows [M+H]⁺ at m/z 793.5 and [M+2H]²⁺ at m/z 397.2 (monoisotopic). MS/MS confirms the 42 Da acetyl shift on N-terminal fragments and the amide on C-terminal fragments.

Impurity profile
Typical checks include incompletely capped forms (non-acetylated or free-acid), which differ by 42 Da or about 1 Da, truncated sequences and counter-ion content.

07

Technical Specifications

Analytical Data & Molecular Properties
Sequence
Ac-Thr-Lys-Pro-Arg-Pro-Gly-Pro-NH₂
Molecular Formula
C₃₅H₆₀N₁₂O₉
CAS Number
Not assigned
Molecular Weight
792.9 g/mol (calculated)
Purity
≥98% (HPLC)
Storage
−20 °C, desiccated
Appearance
White lyophilized powder
Solubility
Soluble in water
08

Cross-Referenced Materials

09

Frequently Asked Questions

How does N-Acetyl Selank Amidate differ from Selank?

It has the same seven-residue sequence, but with an acetyl group on the N-terminus and an amide at the C-terminus. This makes it about 41 Da heavier (792.9 versus 751.9 g/mol) and removes both terminal charges.

Why cap both ends of a peptide?

Free termini are the starting points for aminopeptidases and carboxypeptidases. Capping both ends blocks these enzymes and generally makes short peptides last longer in biological samples.

Does it have a CAS number?

No widely recognised CAS number has been assigned. Identity is confirmed by sequence, accurate mass and MS/MS.

How are the terminal modifications confirmed?

By accurate intact mass and MS/MS. N-terminal fragments carry the 42 Da acetyl shift, and C-terminal fragments show the amide rather than the free acid.

Is its activity the same as Selank’s?

It is generally assumed to follow Selank, but published data on the capped form itself are limited. Direct comparison under the same conditions is recommended.

Is N-Acetyl Selank Amidate intended for human or veterinary use?

No. It is supplied strictly as a reference compound for laboratory and analytical research and is not for human or animal use.

10

How to Cite This Reference

N-Acetyl Selank Amidate Research Reference. (2026). Pure Peptides Labs Research Catalogue. Retrieved from https://purepeptideslabs.net/research-catalogue/neurochemical-research-peptides/n-acetyl-selank-amidate/

Available for Research

Materials listed on this platform are supported by independent testing and published documentation for laboratory research contexts.

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