FGL-S is a synthetic peptide composed of 15 amino acids and described in the scientific literature as a sequence derived from the second fibronectin type III module of the neural cell adhesion molecule (NCAM). NCAM-derived peptides have been examined in experimental research as molecular mimetics that reproduce specific structural motifs of the parent adhesion molecule under controlled laboratory conditions.

Publications referencing FGL-S and related FGL peptides describe their use in non-clinical research contexts involving cellular assays and animal model systems. All reported observations are confined to descriptive and mechanistic investigations and are limited to laboratory-based experimental settings.

No statements regarding human applicability, clinical relevance, or biological outcomes beyond research observation are made.

Source: PubChem

Amino Acid Sequence: H-Glu-Val-Tyr-Val-Val-Ala-Glu-Asn-Gln-Gln-Gly-Lys-Ser-Lys-Ala-OH
Molecular Formula: C₇₁H₁₁₆N₂₀O₂₅
Molecular Weight: 1649.8 g/mol
PubChem CID: 16200289
CAS Number: 499993-62-3
Reported Synonyms: HY-P3281, DA-53184, CS-0655069

FGL-S has been described as a linear peptide whose primary structure reproduces a specific NCAM-associated motif. Structural descriptions are limited to compositional and physicochemical attributes reported in biochemical research sources.

In the scientific literature, FGL-S and related FGL peptides have been referenced in non-clinical research involving cellular cultures, ex-vivo preparations, and animal model studies. These publications describe experimental contexts in which molecular interactions, signaling components, and structural features were observed and recorded.

Reported research contexts include examination of:

• NCAM-associated molecular interactions
• Fibroblast growth factor receptor (FGFR) signaling components
• Neurite morphology and synaptic ultrastructure in experimental models
• Glial cell–associated molecular markers
• Transcriptional responses following experimental perturbation

All reported applications remain confined to descriptive investigation within controlled laboratory research environments.

Mechanistic discussions in preclinical publications describe FGL peptides in relation to neural cell adhesion molecule (NCAM)–associated signaling and fibroblast growth factor receptor (FGFR)–linked intracellular pathways. These pathways have been examined in experimental systems for their involvement in cytoskeletal organization, vesicular dynamics, and transcriptional regulation.

Additional references describe observations involving kinase-associated signaling modules, including MAPK- and PI3K-related cascades, recorded under defined laboratory conditions. All pathway-related descriptions are limited to molecular and biochemical observations within experimental research settings.

Preclinical studies cited in the scientific literature describe observations involving FGL peptides in cellular and non-clinical animal models. Reported observations include measurements of neurite-associated structures, synaptic ultrastructural features, gene expression markers, and signaling-associated proteins documented under defined experimental conditions.

Additional publications describe transcriptional and cellular responses observed following experimental injury or perturbation models. All reported findings remain restricted to the experimental systems employed and do not extend beyond laboratory research contexts.

FGL-S is supplied as a research-grade synthetic peptide material. Identity and composition have been reported as characterized using analytical techniques commonly applied to peptide research materials, including chromatographic and mass spectrometric methods.

Handling, storage, and analytical verification parameters are determined by individual laboratories in accordance with internal research protocols.

The above literature was researched, edited, and organized by Dr. Logan, M.D. Dr. Logan holds a doctorate degree from Case Western Reserve University School of Medicine and a B.S. in molecular biology.

Victor I. Popov, Ph.D. is a senior researcher at the Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino, Russia. His published work focuses on synaptic transmission, presynaptic mechanisms, calcium signaling, and neuronal ultrastructure in experimental research systems.

Dr. Popov is cited solely for attribution of scientific authorship in the referenced literature. No endorsement, affiliation, or advocacy of any product is implied or stated. The purpose of citation is to acknowledge research contributions only.

1. V. I. Popov et al., “A cell adhesion molecule mimetic, FGL peptide, induces alterations in synapse and dendritic spine structure in the dentate gyrus of aged rats,” Eur J Neurosci, vol. 27, no. 2, pp. 301–314, Jan. 2008. doi: 10.1111/j.1460-9568.2007.06004.x.
2. A. Aonurm-Helm et al., “NCAM-mimetic, FGL peptide, restores disrupted FGFR signaling in NCAM-deficient mice,” Brain Res, vol. 1309, pp. 1–8, Jan. 2010.
3. T. Secher et al., “NCAM-derived FGL peptide and postnatal sensorimotor development,” Neuroscience, vol. 141, no. 3, pp. 1289–1299, 2006.
4. R. Anand et al., “Tolerability and pharmacokinetics of the FGLL peptide,” Clin Pharmacokinet, vol. 46, no. 4, pp. 351–358, 2007.
5. X. Wen et al., “Extracellular vesicles and synaptic toxicity models,” Int J Nanomedicine, vol. 20, pp. 4627–4644, 2025.
6. M. V. Pedersen et al., “NCAM-derived peptide modulation following traumatic brain injury,” Neurosci Lett, vol. 437, no. 2, pp. 148–153, 2008.

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