biohacking$bioLLM CA: TBA

database / metabolic

HGH Fragment 176-191

research compound metabolic metabolic modified — mass check n/a

Research reference only. The observations below are recorded in the cited literature. Nothing here is advice or a recommendation, and no dosing information is published on this site.

Sequence

LRIVQCRSVEGSCGF

Leu-Arg-Ile-Val-Gln-Cys-Arg-Ser-Val-Glu-Gly-Ser-Cys-Gly-Phe

1. Leu — Leucine · hydrophobic · hydropathy 3.8 · charge 0L12. Arg — Arginine · positive · hydropathy -4.5 · charge +1R3. Ile — Isoleucine · hydrophobic · hydropathy 4.5 · charge 0I4. Val — Valine · hydrophobic · hydropathy 4.2 · charge 0V5. Gln — Glutamine · polar · hydropathy -3.5 · charge 0Q6. Cys — Cysteine · cysteine · hydropathy 2.5 · charge 0C67. Arg — Arginine · positive · hydropathy -4.5 · charge +1R8. Ser — Serine · polar · hydropathy -0.8 · charge 0S9. Val — Valine · hydrophobic · hydropathy 4.2 · charge 0V10. Glu — Glutamic acid · negative · hydropathy -3.5 · charge −1E11. Gly — Glycine · glycine · hydropathy -0.4 · charge 0G1112. Ser — Serine · polar · hydropathy -0.8 · charge 0S13. Cys — Cysteine · cysteine · hydropathy 2.5 · charge 0C14. Gly — Glycine · glycine · hydropathy -0.4 · charge 0G15. Phe — Phenylalanine · aromatic · hydropathy 2.8 · charge 0F15

Modified molecule. Disulfide-bonded fragment of human growth hormone.

Backbone carries modifications, so computed backbone mass is not comparable to the reported mass of the complete molecule.

Molecular data

Chemical fields come from the PubChem compound record; computed values are derived from the sequence shown above.
molecular formulanot characterised
molecular weight1653.93 Da (computed from sequence)
computed backbone mass1653.93 Da
length15 residues
net charge (pH 7.4)+1
mean hydropathy0.41
half-lifenot characterised
delivery routenot characterised
PubChem CIDnot characterised
PDBnot characterised
UniProt parentP01241

Mechanism

C-terminal GH fragment investigated for effects on adipose tissue.

Reported targets: not established

Experimental structure

No experimental structure of this peptide is deposited in the PDB. Nothing is rendered here — a predicted fold would not be a structure, and this site does not draw one.

Position in the parent protein

exact match at residues 203–217 of Somatotropin (217 aa)

…DDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF

Parent sequence from UniProt P01241. Residues 176-191 of human growth hormone.

Reported effects

Each row is an outcome described in the literature indexed for this peptide. Reported in the cited work — not a claim, not a recommendation.

Reported observations and the corpus they are drawn from.
reported outcomewhere it appears
lipolysisThe 14-Kilodalton Human Growth Hormone Fragment a Potent Inhibitor of Angiog… International journal of molecular sciences 2023

Literature (2)

The 14-Kilodalton Human Growth Hormone Fragment a Potent Inhibitor of Angiogenesis and Tumor Metastasis — International journal of molecular sciences 2023

The 14-kilodalton human growth hormone (14 kDa hGH) N-terminal fragment derived from the proteolytic cleavage of its full-length counterpart has been shown to sustain antiangiogenic potentials. This study investigated the antitumoral and antimetastatic effects of 14 kDa hGH on B16-F10 murine melanoma cells. B16-F10 murine melanoma cells transfected with 14 kDa hGH expression vectors showed a significant reduction in cellular proliferation and migration associated with an increase in cell apoptosis in vitro. In vivo, 14 kDa hGH mitigated tumor growth and metastasis of B16-F10 cells and was associated with a significant reduction in tumor angiogenesis. Similarly, 14 kDa hGH expression reduced human brain microvascular endothelial (HBME) cell proliferation, migration, and tube formation abilities and triggered apoptosis in vitro. The antiangiogenic effects of 14 kDa hGH on HBME cells were a…

open access ↗ · PMID 37240223 · DOI 10.3390/ijms24108877

Human Growth Hormone Fragment 176-191 Peptide Enhances the Toxicity of Doxorubicin-Loaded Chitosan Nanoparticles Against MCF-7 Breast Cancer Cells — Drug design, development and therapy 2022

IntroductionNumerous drugs with potent toxicity against cancer cells are available for treating malignancies, but therapeutic efficacies are limited due to their inefficient tumor targeting and deleterious effects on non-cancerous tissue. Therefore, two improvements are mandatory for improved chemotherapy 1) novel delivery techniques that can target cancer cells to deliver anticancer drugs and 2) methods to specifically enhance drug efficacy within tumors. The loading of inert drug carriers with anticancer agents and peptides which are able to bind (target) tumor-related proteins to enhance tumor drug accumulation and local cytotoxicity is a most promising approach.ObjectiveTo evaluate the anticancer efficacy of Chitosan nanoparticles loaded with human growth hormone hGH fragment 176-191 peptide plus the clinical chemotherapeutic doxorubicin in comparison with Chitosan loaded with doxoru…

open access ↗ · PMID 35783198 · DOI 10.2147/dddt.s367586

Related

Teduglutide

metabolic · 8 citations

Pramlintide

metabolic · 8 citations

Leptin fragment (116-130)

metabolic · 6 citations

AOD-9604

metabolic · 8 citations

Vilon

longevity · 8 citations

Epitalon

longevity · 8 citations