Gly-Gly-Phe-OH - CAS 6234-26-0

Gly-Gly-Phe-OH - CAS 6234-26-0 Catalog number: BADC-01588

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Gly-Gly-Phe-OH is a cleavable peptide linker that is widely used in the development of antibody-drug conjugates. Furthermore, Gly-Gly-Phe-OH brings hope to the field of oncology research, having demonstrated its ability as a targeted therapeutic moiety to selectively target tumor cells with high precision.

Category
ADCs Linker
Product Name
Gly-Gly-Phe-OH
CAS
6234-26-0
Catalog Number
BADC-01588
Molecular Formula
C13H17N3O4
Molecular Weight
279.30
Purity
≥ 99% (HPLC)
Gly-Gly-Phe-OH

Ordering Information

Catalog Number Size Price Quantity
BADC-01588 -- $-- Inquiry
Description
Gly-Gly-Phe-OH is a cleavable peptide linker that is widely used in the development of antibody-drug conjugates. Furthermore, Gly-Gly-Phe-OH brings hope to the field of oncology research, having demonstrated its ability as a targeted therapeutic moiety to selectively target tumor cells with high precision.
Synonyms
Glycyl-glycyl-L-phenylalanine
IUPAC Name
(2S)-2-[[2-[(2-aminoacetyl)amino]acetyl]amino]-3-phenylpropanoic acid
Canonical SMILES
C1=CC=C(C=C1)CC(C(=O)O)NC(=O)CNC(=O)CN
InChI
InChI=1S/C13H17N3O4/c14-7-11(17)15-8-12(18)16-10(13(19)20)6-9-4-2-1-3-5-9/h1-5,10H,6-8,14H2,(H,15,17)(H,16,18)(H,19,20)/t10-/m0/s1
InChIKey
KAJAOGBVWCYGHZ-JTQLQIEISA-N
Density
1.296±0.06 g/cm3(Predicted)
Melting Point
228-230 °C (dec.)
Appearance
White powder
Storage
Store at -20°C
Boiling Point
647.1±55.0 °C(Predicted)

Gly-Gly-Phe-OH is a tripeptide composed of two glycine residues and one phenylalanine residue. Its simplicity and versatility make it an important tool in peptide synthesis, with applications in both basic research and drug development. The glycine residues provide flexibility to the peptide, while the phenylalanine acts as a bulky, aromatic side chain that can interact with hydrophobic regions of proteins or receptors. This peptide is often used as a model compound in studies of protein-protein interactions and in the design of peptide-based therapeutics. Its role as a basic building block for more complex peptide sequences is vital in exploring structure-activity relationships and optimizing bioactivity in drug discovery.

In drug development, Gly-Gly-Phe-OH is employed as a linker or spacer in the synthesis of peptide-drug conjugates (PDCs). These conjugates are designed to deliver active pharmaceutical agents directly to target cells, enhancing the therapeutic efficacy while minimizing off-target effects. The inclusion of phenylalanine in the tripeptide allows for selective interactions with receptors or enzymes, which can improve the specificity of drug delivery. The glycine residues, being small and neutral, provide the necessary flexibility to ensure that the conjugate retains its ability to bind to the target molecule effectively. This makes Gly-Gly-Phe-OH useful in the development of targeted therapies, particularly in cancer treatment, where precise drug delivery to tumor cells is crucial.

Gly-Gly-Phe-OH also has applications in the study of enzyme catalysis and molecular recognition. The phenylalanine residue, with its aromatic ring, can engage in hydrophobic interactions and π-π stacking with other aromatic groups, making it useful for studying enzyme-substrate binding or protein-ligand interactions. Researchers use this tripeptide to model and probe enzyme specificity, as well as to identify key residues involved in enzyme catalysis. Furthermore, it can be incorporated into peptide libraries to investigate peptide-based inhibitors or activators of enzymes, thereby advancing the development of enzyme-targeted therapies for diseases such as cancer, Alzheimer's, or metabolic disorders.

In the field of biomaterials and tissue engineering, Gly-Gly-Phe-OH is utilized for functionalizing surfaces or scaffolds. The phenylalanine residue can interact with hydrophobic domains of proteins or other biomolecules, facilitating the immobilization of therapeutic peptides or proteins onto solid surfaces. The glycine residues ensure flexibility in the peptide chain, allowing for better incorporation into diverse biomaterials. This property is valuable in regenerative medicine, where functionalized surfaces can be used to promote cell adhesion, tissue growth, and the controlled release of bioactive molecules, aiding in tissue repair and wound healing.

1. β-Sheet to Helical-Sheet Evolution Induced by Topochemical Polymerization: Cross-α-Amyloid-like Packing in a Pseudoprotein with Gly-Phe-Gly Repeats
Kuntrapakam Hema, Kana M Sureshan Angew Chem Int Ed Engl. 2020 Jun 2;59(23):8854-8859. doi: 10.1002/anie.201914975. Epub 2020 Mar 25.
Protein-mimics are of great interest for their structure, stability, and properties. We are interested in the synthesis of protein-mimics containing triazole linkages as peptide-bond surrogate by topochemical azide-alkyne cycloaddition (TAAC) polymerization of azide- and alkyne-modified peptides. The rationally designed dipeptide N3 -CH2 CO-Phe-NHCH2 CCH (1) crystallized in a parallel β-sheet arrangement and are head-to-tail aligned in a direction perpendicular to the β-sheet-direction. Upon heating, crystals of 1 underwent single-crystal-to-single-crystal polymerization forming a triazole-linked pseudoprotein with Gly-Phe-Gly repeats. During TAAC polymerization, the pseudoprotein evolved as helical chains. These helical chains are laterally assembled by backbone hydrogen bonding in a direction perpendicular to the helical axis to form helical sheets. This interesting helical-sheet orientation in the crystal resembles the cross-α-amyloids, where α-helices are arranged laterally as sheets.
2. A systematic study of the valence electronic structure of cyclo(Gly-Phe), cyclo(Trp-Tyr) and cyclo(Trp-Trp) dipeptides in the gas phase
Elena Molteni, et al. Phys Chem Chem Phys. 2021 Dec 8;23(47):26793-26805. doi: 10.1039/d1cp04050b.
The electronic energy levels of cyclo(glycine-phenylalanine), cyclo(tryptophan-tyrosine) and cyclo(tryptophan-tryptophan) dipeptides are investigated with a joint experimental and theoretical approach. Experimentally, valence photoelectron spectra in the gas phase are measured using VUV radiation. Theoretically, we first obtain low-energy conformers through an automated conformer-rotamer ensemble sampling scheme based on tight-binding simulations. Then, different first principles computational schemes are considered to simulate the spectra: Hartree-Fock (HF), density functional theory (DFT) within the B3LYP approximation, the quasi-particle GW correction, and the quantum-chemistry CCSD method. Theory allows assignment of the main features of the spectra. A discussion on the role of electronic correlation is provided, by comparing computationally cheaper DFT scheme (and GW) results with the accurate CCSD method.
The molarity calculator equation

Mass (g) = Concentration (mol/L) × Volume (L) × Molecular Weight (g/mol)

The dilution calculator equation

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)

This equation is commonly abbreviated as: C1V1 = C2V2

Historical Records: Gly-Gly-Phe-OH
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