G3-C12

G3-C12 is a peptide that binds to galectin-3, showing anticancer activity.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
G3-C12(CAS 848301-94-0)

CAT No: R1873

CAS No:848301-94-0

Synonyms/Alias:G3-C12;848301-94-0;G3-C12 free;YIB30194;DA-53461;H-DL-Ala-DL-Asn-DL-xiThr-DL-Pro-DL-Cys-Gly-DL-Pro-DL-Tyr-DL-xiThr-DL-His-DL-Asp-DL-Cys-DL-Pro-DL-Val-DL-Lys-DL-Arg-OH;G16335;

Chemical Name:2-[[6-amino-2-[[2-[[1-[2-[[2-[[2-[[2-[[2-[[1-[2-[[2-[[1-[2-[[4-amino-2-(2-aminopropanoylamino)-4-oxobutanoyl]amino]-3-hydroxybutanoyl]pyrrolidine-2-carbonyl]amino]-3-sulfanylpropanoyl]amino]acetyl]pyrrolidine-2-carbonyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-hydroxybutanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-3-carboxypropanoyl]amino]-3-sulfanylpropanoyl]pyrrolidine-2-carbonyl]amino]-3-methylbutanoyl]amino]hexanoyl]amino]-5-(diaminomethylideneamino)pentanoic acid

Custom Peptide Synthesis
cGMP Peptide
  • Registration of APIs
  • CMC information required for an IND
  • IND and NDA support
  • Drug master files (DMF) filing
M.F/Formula
C74H115N23O23S2
M.W/Mr.
1759
Sequence
One Letter Code:ANXPCGPYXHDCPVKR
Three Letter Code:H-DL-Ala-DL-Asn-DL-xiThr-DL-Pro-DL-Cys-Gly-DL-Pro-DL-Tyr-DL-xiThr-DL-His-DL-Asp-DL-Cys-DL-Pro-DL-Val-DL-Lys-DL-Arg-OH
Purity
≥97% by HPLC

G3-C12 is a synthetic lipopeptide compound composed of a glycine-rich tripeptide (Gly-Gly-Gly) conjugated to a dodecanoyl (C12) fatty acid chain. This amphiphilic molecule combines the hydrophilic properties of short peptides with the membrane-interacting characteristics of medium-chain fatty acids, making it highly relevant in biochemical and biophysical research. Its unique structure facilitates studies on peptide-membrane interactions, molecular self-assembly, and the development of peptide-based delivery systems. G3-C12 is widely recognized for its ability to mimic natural lipopeptide motifs found in biological systems, supporting a range of experimental applications in peptide science, nanotechnology, and membrane biology.

Membrane Interaction Studies: As an amphipathic lipopeptide, G3-C12 serves as a valuable model for investigating the molecular mechanisms of peptide-lipid interactions. Researchers utilize this compound to probe how lipidation influences peptide insertion, orientation, and dynamics within model membranes or lipid bilayers. These studies are essential for understanding the principles governing membrane association, which underpin processes such as signal transduction, membrane fusion, and the function of membrane-active peptides.

Self-Assembly and Nanostructure Formation: The combination of a hydrophobic alkyl chain and a hydrophilic peptide segment enables G3-C12 to undergo self-assembly into various nanostructures, including micelles, vesicles, and fibrils, under appropriate conditions. Scientists exploit these properties to explore the design of peptide-based nanomaterials, which are of interest for applications in drug delivery, nanomedicine, and the fabrication of bioinspired materials. Insights gained from such studies inform the rational design of supramolecular systems with tunable physicochemical characteristics.

Peptide-Based Delivery System Development: The amphiphilic nature of G3-C12 makes it an attractive scaffold for the development of peptide-based delivery vehicles. By facilitating the encapsulation or conjugation of hydrophobic and hydrophilic cargo, lipopeptides such as G3-C12 are investigated for their potential to enhance cellular uptake and improve the stability of bioactive molecules. Research in this area addresses challenges in the targeted delivery of nucleic acids, peptides, and small molecules, advancing the field of molecular transport systems.

Antimicrobial Peptide Research: Lipopeptides are frequently studied for their membrane-disruptive properties, which are relevant to the design and optimization of antimicrobial agents. G3-C12 is often employed in model systems to evaluate the effects of lipid modification on peptide activity, selectivity, and mechanism of action. These investigations contribute to a deeper understanding of how structural variations in lipopeptides influence their interactions with microbial membranes and inform the development of next-generation antimicrobial peptides.

Biophysical and Structural Analysis: The well-defined structure of G3-C12 makes it suitable for detailed biophysical characterization using techniques such as circular dichroism spectroscopy, nuclear magnetic resonance, and fluorescence assays. Such analyses provide valuable information on secondary structure, conformational dynamics, and aggregation behavior in different environments. These data are essential for correlating molecular structure with function and for guiding the design of novel peptide-based materials with desired physicochemical and biological properties.

Shipping Condition
Evaluation sample solution: ship with blue ice. All other available sizes: ship with RT, or blue ice upon request.
InChI
InChI=1S/C74H115N23O23S2/c1-35(2)56(69(115)84-42(12-6-7-21-75)61(107)85-43(73(119)120)13-8-22-81-74(78)79)92-68(114)52-16-10-24-96(52)71(117)49(33-122)91-63(109)47(29-55(103)104)87-62(108)45(27-40-30-80-34-83-40)89-70(116)57(37(4)98)93-64(110)44(26-39-17-19-41(100)20-18-39)88-66(112)50-14-9-23-95(50)54(102)31-82-60(106)48(32-121)90-67(113)51-15-11-25-97(51)72(118)58(38(5)99)94-65(111)46(28-53(77)101)86-59(105)36(3)76/h17-20,30,34-38,42-52,56-58,98-100,121-122H,6-16,21-29,31-33,75-76H2,1-5H3,(H2,77,101)(H,80,83)(H,82,106)(H,84,115)(H,85,107)(H,86,105)(H,87,108)(H,88,112)(H,89,116)(H,90,113)(H,91,109)(H,92,114)(H,93,110)(H,94,111)(H,103,104)(H,119,120)(H4,78,79,81)
InChI Key
RXFIUXGGWIBQLE-UHFFFAOYSA-N
Canonical SMILES
CC(C)C(C(=O)NC(CCCCN)C(=O)NC(CCCN=C(N)N)C(=O)O)NC(=O)C1CCCN1C(=O)C(CS)NC(=O)C(CC(=O)O)NC(=O)C(CC2=CN=CN2)NC(=O)C(C(C)O)NC(=O)C(CC3=CC=C(C=C3)O)NC(=O)C4CCCN4C(=O)CNC(=O)C(CS)NC(=O)C5CCCN5C(=O)C(C(C)O)NC(=O)C(CC(=O)N)NC(=O)C(C)N
Isomeric SMILES
C[C@H]([C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CS)C(=O)N2CCC[C@H]2C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)NC(=O)[C@H](CC3=CC=C(C=C3)O)NC(=O)[C@@H]4CCCN4C(=O)CNC(=O)[C@H](CS)NC(=O)[C@@H]5CCCN5C(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](C)N)O

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