How does growth hormone releasing hexapeptide self-assemble in nanotubes?

Santana H, Avila CL, Cabrera I, Páez R, Falcón V, Pessoa A Jr, Ventosa N, Veciana J, Itri R, Barbosa LR

Soft matter1 Dec 2014Cited by 6 (Europe PMC)

PMID25325399DOI10.1039/c4sm01693aPepBankPUB-25325399

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 study9

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone9

In this study, GHRP-6 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 GHRP-6.

01LabNot a test of GHRP-6 aloneIn vitro (cell-free)Other
In aqueous solution, GHRP‑6 formed long nanotubes at pH 7.0 and 22 °C.
In plain wordsIn lab tests, GHRP‑6 formed long nanotubes in water.
Peptide
GHRP-6
Outcome
Not applicableNanotube formation
Study
n: not reported in source
Outcome group
Peptide structure and chemistry · Pharmacology
Source sentences
Summary
In the present study, we demonstrate that GHRP-6 dispersed in aqueous solution, at pH 7.0, room temperature of 22 °C, is able to form long nanotubes, which is evidenced by combining small angle X-ray scattering (SAXS), transmission electron microscopy and molecular dynamics simulation results.
In this study, GHRP-6 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 GHRP-6.
Report a problemFND-2532539901
02LabNot a test of GHRP-6 aloneIn vitro (cell-free)Other
In aqueous solution, GHRP‑6 nanotubes had an inner cross-section of 6.7(2) nm.
In plain wordsIn lab tests, GHRP‑6 nanotubes had an inner cross-section of 6.7(2) nm.
Peptide
GHRP-6
Outcome
Not applicableNanotube inner cross-section
Study
n: not reported in source
Outcome group
Peptide structure and chemistry · Pharmacology
Measurements
Inner cross-section
6.7 nm
nanotubes, reported as 6.7(2) nm
Source sentences
Summary
Such nanotubes possess inner and outer cross-sections equal to 6.7(2) nm and 13.4(5) nm, respectively.
In this study, GHRP-6 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 GHRP-6.
Report a problemFND-2532539902
03LabNot a test of GHRP-6 aloneIn vitro (cell-free)Other
At higher peptide concentration, GHRP‑6 nanotubes formed hexagonal-like packing with a center-to-center distance of approximately 15 nm.
In plain wordsIn lab tests, higher GHRP‑6 concentrations produced hexagonal-like packing of nanotubes.
Peptide
GHRP-6
Outcome
Not applicableConcentration-dependent nanotube packing
Study
n: not reported in source
Outcome group
Peptide structure and chemistry · Pharmacology
Measurements
Center-to-center distance
≈ 15 nm
hexagonal-like packing at increased peptide concentration
Source sentences
Summary
On increasing the peptide concentration, the long nanotubes self-arrange in solution displaying a bi-dimensional hexagonal-like packing in the SAXS curves, with a center-to-center distance of ∼15 nm.
In this study, GHRP-6 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 GHRP-6.
Report a problemFND-2532539907
04LabNot a test of GHRP-6 aloneIn vitro (cell-free)Other
The GHRP‑6 nanostructure remained stable after transfer from solution to a solid support.
In plain wordsIn lab tests, GHRP‑6 nanostructures remained intact after transfer to a solid support.
Peptide
GHRP-6
Outcome
Not applicableNanostructure stability
Study
n: not reported in source
Outcome group
Peptide structure and chemistry · Pharmacology
Source sentences
Summary
Further, we also show that the nanostructure formed in solution is quite stable and is preserved following transfer to a solid support.
In this study, GHRP-6 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 GHRP-6.
Report a problemFND-2532539908
05LabNot a test of GHRP-6 aloneIn vitro (cell-free)Other
In aqueous solution, GHRP‑6 nanotubes had an outer cross-section of 13.4(5) nm.
In plain wordsIn lab tests, GHRP‑6 nanotubes had an outer cross-section of 13.4(5) nm.
Peptide
GHRP-6
Outcome
Not applicableNanotube outer cross-section
Study
n: not reported in source
Outcome group
Peptide structure and chemistry · Pharmacology
Measurements
Outer cross-section
13.4 nm
nanotubes, reported as 13.4(5) nm
Source sentences
Summary
Such nanotubes possess inner and outer cross-sections equal to 6.7(2) nm and 13.4(5) nm, respectively.
In this study, GHRP-6 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 GHRP-6.
Report a problemFND-2532539909
06Computer modelNot a test of GHRP-6 aloneIn silicoMechanism
Molecular dynamics simulations showed GHRP‑6 self-assembly into a partially interdigitated structure in aqueous solution.
In plain wordsComputer simulations showed GHRP‑6 molecules forming a partially interdigitated structure in water.
Peptide
GHRP-6
Outcome
Not applicableSelf-assembly structure
Study
n: not reported in source
Outcome group
Peptide structure and chemistry · Pharmacology
Source sentences
Summary
The mechanism of peptide self-assembly was determined by molecular dynamics simulations revealing that the peptides self-assemble like amphiphilic molecules in aqueous solution in a partially interdigitated structure.
In this study, GHRP-6 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 GHRP-6.
Report a problemFND-2532539903
07Computer modelNot a test of GHRP-6 aloneIn silicoMechanism
Simulations placed the GHRP‑6 amino terminus at the peptide-water interface and its capped carboxy terminus in the hydrophobic core.
In plain wordsComputer simulations placed the two ends of GHRP‑6 in different regions of the structure.
Peptide
GHRP-6
Outcome
Not applicableTerminal positioning
Study
n: not reported in source
Outcome group
Peptide structure and chemistry · Pharmacology
Source sentences
Summary
In this case, the position of the positively charged amino terminus is located at the peptide-water interface, whereas the neutral NH2-capped carboxy terminus remains buried at the hydrophobic core.
In this study, GHRP-6 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 GHRP-6.
Report a problemFND-2532539904
08Computer modelNot a test of GHRP-6 aloneIn silicoMechanism
Simulations placed the positive charge of the GHRP‑6 Lys-6 side chain near the cylinder surface.
In plain wordsComputer simulations placed the lysine side-chain charge of GHRP‑6 near the tube surface.
Peptide
GHRP-6
Outcome
Not applicableLysine side-chain positioning
Study
n: not reported in source
Outcome group
Peptide structure and chemistry · Pharmacology
Source sentences
Summary
In contrast, the long side chain of Lys-6 stretches out of the hydrophobic core positioning its positive charge near the cylinder surface.
In this study, GHRP-6 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 GHRP-6.
Report a problemFND-2532539905
09Computer modelNot a test of GHRP-6 aloneIn silicoMechanism
GHRP‑6 nanotube configuration reflected aromatic hydrophobic interactions and electrostatic repulsion between cationic charges.
In plain wordsComputer simulations linked GHRP‑6 tube structure to hydrophobic interactions and repulsion between positive charges.
Peptide
GHRP-6
Outcome
Not applicableNanotube configuration mechanism
Study
n: not reported in source
Outcome group
Peptide structure and chemistry · Pharmacology
Source sentences
Summary
The peptide configuration in the nanotube wall comes from the interplay between the hydrophobic interactions of the aromatic side chains of GHRP-6 and the electrostatic repulsion of its cationic charges.
In this study, GHRP-6 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 GHRP-6.
Report a problemFND-2532539906

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
21 Oct 2026, 15:58 UTC
Study results updated
Version 1
9 Oct 2026, 03:13 UTC
First added · source update from Europe PMC

Subjects

Terms as the source lists them.

Publication types

MeSH terms

PepBank is a research reference. Talk to a doctor before you use any peptide.