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Somatostatin-14

research compound hormone endocrinegastrointestinalnervous modified — mass check n/a
SSOOOOOOOOOOOOOOOOOOONNNNNNNNNNNNNNNNNNHHHHHHHHHHHHHHHHHHHHHHHHHH
115 heavy atoms · 224 bonds · drag to pan, scroll to zoom C76O19N18S2

Skeletal structure drawn from the computed atomic coordinates in PubChem CID 16129706. Carbons are implicit vertices; hydrogens on carbon are suppressed, as in any structural formula. Nothing here is estimated — every atom sits where PubChem placed it.

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

AGCKNFFWKTFTSC

Ala-Gly-Cys-Lys-Asn-Phe-Phe-Trp-Lys-Thr-Phe-Thr-Ser-Cys

1. Ala — Alanine · hydrophobic · hydropathy 1.8 · charge 0A12. Gly — Glycine · glycine · hydropathy -0.4 · charge 0G3. Cys — Cysteine · cysteine · hydropathy 2.5 · charge 0C4. Lys — Lysine · positive · hydropathy -3.9 · charge +1K5. Asn — Asparagine · polar · hydropathy -3.5 · charge 0N6. Phe — Phenylalanine · aromatic · hydropathy 2.8 · charge 0F67. Phe — Phenylalanine · aromatic · hydropathy 2.8 · charge 0F8. Trp — Tryptophan · aromatic · hydropathy -0.9 · charge 0W9. Lys — Lysine · positive · hydropathy -3.9 · charge +1K10. Thr — Threonine · polar · hydropathy -0.7 · charge 0T11. Phe — Phenylalanine · aromatic · hydropathy 2.8 · charge 0F1112. Thr — Threonine · polar · hydropathy -0.7 · charge 0T13. Ser — Serine · polar · hydropathy -0.8 · charge 0S14. Cys — Cysteine · cysteine · hydropathy 2.5 · charge 0C14

Modified molecule. Cyclic via a Cys3–Cys14 disulfide.

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 formulaC76H104N18O19S2
molecular weight1637.9 Da (PubChem)
computed backbone mass1639.91 Da
length14 residues
net charge (pH 7.4)+2
mean hydropathy0.03
half-lifenot characterised
delivery routenot characterised
PubChem CID16129706
PDBnot characterised
UniProt parentP61278

Mechanism

Pan-somatostatin receptor agonist; broad inhibitor of endocrine secretion.

Reported targets: SSTR1-5

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 103–116 of Somatostatin (116 aa)

…QDEMRLELQRSANSNPAMAPRERKAGCKNFFWKTFTSC

Parent sequence from UniProt P61278. SST-14 and SST-28 derive from prosomatostatin.

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
GH suppressionSimultaneous LC-MS determination of glucose regulatory peptides secreted by … Electrophoresis 2023
insulin and glucagon suppressionBis(Disulfide)-Bridged Somatostatin-14 Analogs and Their [<sup>111</sup>In]I… International journal of molecular sciences 2024

Literature (7)

Simultaneous LC-MS determination of glucose regulatory peptides secreted by stem cell-derived islet organoids — Electrophoresis 2023

abstract not reproduced — this record is not open-access, so it is linked rather than copied.

publisher record ↗ · PMID 37574258 · DOI 10.1002/elps.202300095

Bis(Disulfide)-Bridged Somatostatin-14 Analogs and Their [<sup>111</sup>In]In-Radioligands: Synthesis and Preclinical Profile — International journal of molecular sciences 2024

The overexpression of one or more somatostatin receptors (SST1-5R) in human tumors has provided an opportunity for diagnosis and therapy with somatostatin-like radionuclide carriers. The application of "pansomatostatin" analogs is expected to broaden the clinical indications and upgrade the diagnostic/therapeutic efficacy of currently applied SST2R-prefering radioligands. In pursuit of this goal, we now introduce two bicyclic somatostatin-14 (SS14) analogs, AT5S (DOTA-Ala1-Gly2-c[Cys3-Lys4-Asn5-c[Cys6-Phe7-DTrp8-Lys9-Thr10-Cys11]-Thr12-Ser13-Cys14]) and AT6S (DOTA-Ala1-Gly2-c[Cys3-Lys4-c[Cys5-Phe6-Phe7-DTrp8-Lys9-Thr10-Phe11-Cys12]-Ser13-Cys14]), suitable for labeling with trivalent radiometals and designed to sustain in vivo degradation. Both AT5S and AT6S and the respective [111In]In-AT5S and [111In]In-AT6S were evaluated in a series of in vitro assays, while radioligand stability and …

open access ↗ · PMID 38339198 · DOI 10.3390/ijms25031921

Simultaneous LC-MS determination of glucose regulatory peptides secreted by stem cell-derived islet organoids — bioRxiv 2023

abstract not reproduced — this record is not open-access, so it is linked rather than copied.

publisher record ↗ · DOI 10.1101/2023.06.12.544566

Structural basis for activation of somatostatin receptor 5 by cyclic neuropeptide agonists — Proceedings of the National Academy of Sciences of the United States of America 2024

Somatostatin receptor 5 (SSTR5) is an important G protein-coupled receptor and drug target for neuroendocrine tumors and pituitary disorders. This study presents two high-resolution cryogenicelectron microscope structures of the SSTR5-Gi complexes bound to the cyclic neuropeptide agonists, cortistatin-17 (CST17) and octreotide, with resolutions of 2.7 Å and 2.9 Å, respectively. The structures reveal that binding of these peptides causes rearrangement of a "hydrophobic lock", consisting of residues from transmembrane helices TM3 and TM6. This rearrangement triggers outward movement of TM6, enabling Gαi protein engagement and receptor activation. In addition to hydrophobic interactions, CST17 forms conserved polar contacts similar to somatostatin-14 binding to SSTR2, while further structural and functional analysis shows that extracellular loops differently recognize CST17 and octreotide. …

open access ↗ · PMID 38885377 · DOI 10.1073/pnas.2321710121

Lipid membrane-mediated assembly of the functional amyloid-forming peptide Somatostatin-14 — Biophysical chemistry 2022

abstract not reproduced — this record is not open-access, so it is linked rather than copied.

publisher record ↗ · PMID 35635892 · DOI 10.1016/j.bpc.2022.106830

Physiology, Somatostatin — StatPearls Publishing, Treasure Island (FL) 2026

Somatostatin is a cyclic peptide with potent regulatory effects throughout the body. Also known as growth hormone–inhibiting hormone, it is produced in multiple locations, including the gastrointestinal tract, pancreas, hypothalamus, and central nervous system. Two active forms of the peptide exist, comprising 14 and 28 amino acids, respectively. The 2 isoforms have considerable overlap in activity and differ primarily in their sites of action. The shorter isoform, somatostatin 14, acts primarily in the brain, whereas the longer isoform, somatostatin 28, acts predominantly in the gastrointestinal tract. Somatostatin has a half-life of 1 to 3 min. Somatostatin produces predominantly neuroendocrine inhibitory effects across multiple systems. The peptide inhibits gastrointestinal, endocrine, exocrine pancreatic, and pituitary secretions and modulates neurotransmission and memory formation i…

open access ↗ · PMID 30855911

Gastrin: a new branch of the gastropancreatic axis that can explain the effect of sleeve gastrectomy on glucose metabolism — Journal of gastrointestinal surgery : official journal of the Society for Surgery of the Alimentary Tract 2024

abstract not reproduced — this record is not open-access, so it is linked rather than copied.

publisher record ↗ · PMID 38583887 · DOI 10.1016/j.gassur.2024.02.015

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