Product Name: GGGGSGGGGS
Sequence: Gly-Gly-Gly-Gly-Ser-Gly-Gly-Gly-Gly-Ser
Purity: 95%
Storage : Sealed storage, away from moisture
CAS.NO.: 192805-56-4
CHEMICAl FORMULA: C22H36N10O13
Molarmass: 648.58
SMILES: C([C@@H](C(=O)NCC(=O)NCC(=O)NCC(=O)NCC(=O)N[C@@H](CO)C(=O)O)NC(=O)CNC(=O)CNC(=O)CNC(=O)CN)O
IUPACNAME: (2S)-2-[[2-[[2-[[2-[[2-[[(2S)-2-[[2-[[2-[[2-[(2-aminoacetyl)amino]acetyl]amino]acetyl]amino]acetyl]amino]-3-hydroxypropanoyl]amino]acetyl]amino]acetyl]amino]acetyl]amino]acetyl]amino]-3-hydroxypropanoic acid
INCHIKEY: YBRPVOYXPRXYEC-RYUDHWBXSA-N
INCHI: InChI=1S/C22H36N10O13/c23-1-13(35)24-2-14(36)25-4-16(38)28-7-19(41)31-11(9-33)21(43)30-6-18(40)27-3-15(37)26-5-17(39)29-8-20(42)32-12(10-34)22(44)45/h11-12,33-34H,1-10,23H2,(H,24,35)(H,25,36)(H,26,37)(H,27,40)(H,28,38)(H,29,39)(H,30,43)(H,31,41)(H,32,42)(H,44,45)/t11-,12-/m0/s1
Application: GGGGSGGGGS is a chimeric peptide sequence composed of glycine- and serine-rich residues, designed for biomaterial interaction and membrane-binding research. This flexible peptide can efficiently bind to small intestinal submucosa (SIS) membranes, making it useful for studies involving extracellular matrix-derived scaffolds, tissue engineering materials, and peptide-functionalized biomaterials. GGGGSGGGGS is valuable for investigating peptide–membrane interactions, scaffold modification, and biological responses under infectious or inflammatory conditions. Its simple, flexible structure supports applications in regenerative medicine, biomaterial design, wound repair research, and studies focused on improving peptide-mediated targeting or functionalization of SIS-based membranes.
Current Research: GGGGSGGGGS is a glycine- and serine-rich chimeric peptide composed of four peptide units and designed for biomaterial interaction research. The sequence contains repeated glycine residues separated by serine, giving it a flexible, hydrophilic, linker-like character. This type of peptide motif is frequently useful in biological materials research because glycine-rich sequences can provide conformational mobility, while serine contributes polarity and aqueous compatibility. GGGGSGGGGS is especially notable for its ability to efficiently bind small intestinal submucosa, or SIS, membranes, making it a valuable reagent for scaffold functionalization, tissue repair studies, infection-related models, and inflammation-focused biomaterial research. Small intestinal submucosa is an extracellular matrix-rich biological scaffold widely studied in regenerative medicine and tissue engineering. SIS membranes contain structural and bioactive matrix components that can support cell attachment, remodeling, tissue integration, and wound repair research. Because SIS-based materials are used as model scaffolds in tissue regeneration and barrier repair studies, peptides that bind SIS membranes can help researchers modify scaffold surfaces with functional molecules, imaging tags, antimicrobial agents, growth factors, immune-modulating peptides, or cell-guidance sequences. GGGGSGGGGS provides a compact peptide tool for improving localization or retention of functional components on SIS membranes. A major application of GGGGSGGGGS is SIS membrane binding research. Researchers may use this peptide to study how short chimeric peptide motifs interact with extracellular matrix-derived biomaterials. Binding assays can be performed using fluorescently labeled peptide, biotinylated peptide, peptide-conjugated nanoparticles, or peptide-linked proteins. Readouts may include fluorescence imaging, confocal microscopy, ELISA-like detection, surface retention assays, wash-resistance testing, and quantitative binding analysis. These studies help define whether GGGGSGGGGS can serve as a scaffold-anchoring motif for more complex biomaterial constructs. GGGGSGGGGS is also useful in biomaterial functionalization. SIS membranes and related extracellular matrix scaffolds often require surface modification to introduce specific biological functions. A peptide that binds SIS can be incorporated into fusion peptides or conjugates containing antimicrobial sequences, anti-inflammatory motifs, cell adhesion ligands, enzyme-sensitive linkers, cytokine-binding domains, or imaging probes. In this way, GGGGSGGGGS can function as a targeting or anchoring component that helps connect a functional payload to the SIS scaffold. In tissue engineering, scaffold-binding peptides are valuable because they can improve spatial control. Instead of allowing soluble factors to diffuse rapidly away from a repair site, scaffold-binding motifs can help retain bioactive molecules near the material surface. GGGGSGGGGS may therefore support research into localized delivery, controlled retention, and surface-associated activity on SIS membranes. Potential applications include wound healing models, soft tissue repair studies, mucosal barrier research, and extracellular matrix remodeling assays. The peptide is also relevant to infection research. SIS membranes may be used in models involving tissue repair under microbial challenge, contaminated wounds, host-pathogen interaction, or antimicrobial scaffold development. GGGGSGGGGS can be used to anchor antimicrobial peptides, antibacterial coatings, immune-modulating molecules, or detection probes to SIS membranes. Researchers can evaluate bacterial adhesion, biofilm formation, antimicrobial activity, scaffold colonization, and peptide retention under biologically relevant wash conditions. Common readouts may include colony-forming unit counts, biofilm biomass staining, live/dead bacterial imaging, scanning electron microscopy, and inflammatory mediator analysis. Inflammation research is another important area. Biomaterial implantation, infection, and tissue injury can activate inflammatory pathways involving macrophages, neutrophils, fibroblasts, epithelial cells, endothelial cells, and cytokine networks. GGGGSGGGGS-functionalized SIS membranes may be used to study how scaffold-bound peptide constructs affect inflammatory cell recruitment, cytokine release, macrophage polarization, oxidative stress, matrix remodeling, and barrier restoration. Researchers may measure TNF-α, IL-1β, IL-6, IL-10, chemokines, nitric oxide, prostaglandins, and tissue remodeling markers depending on the model. Because GGGGSGGGGS is glycine- and serine-rich, it may also be useful as a flexible spacer in fusion designs. When attached to another peptide or protein, it may help reduce steric hindrance between the SIS-binding component and the functional domain. This can improve accessibility of an antimicrobial, adhesive, enzymatic, fluorescent, or immunological motif. Researchers may compare constructs with and without GGGGSGGGGS to determine whether the sequence improves scaffold binding, biological activity, or retention. In peptide engineering workflows, GGGGSGGGGS can support structure-function studies of SIS-binding motifs. Researchers may modify the sequence length, repeat number, serine placement, terminal chemistry, or conjugation format to optimize binding strength and scaffold compatibility. Variants can be compared for SIS membrane affinity, wash stability, solubility, protease resistance, and compatibility with payload attachment. Experimental controls should include SIS membrane alone, peptide-free scaffold, scrambled peptide, unrelated glycine-serine peptide, functional payload without GGGGSGGGGS, and labeled peptide controls. For infection or inflammation models, researchers should also include untreated scaffold, positive inflammatory stimulus, antimicrobial comparator, cell viability testing, and endotoxin assessment where appropriate. Binding should be evaluated under relevant buffer, serum, pH, enzyme, and mechanical wash conditions because scaffold interaction can change in biological environments. Overall, GGGGSGGGGS is a useful chimeric peptide for SIS membrane and biomaterial research. It supports small intestinal submucosa membrane binding studies, scaffold functionalization, tissue engineering, infection-related biomaterial models, inflammatory condition research, localized delivery design, peptide–payload anchoring, and development of flexible peptide-based strategies for extracellular matrix scaffold modification.
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