35665-38-4

Basic information

• Product Name: Fmoc-Gly-Gly-OH
• Synonyms: FMOC-GLYCYL-GLYCINE;FMOC-GLY-GLY-OH;N-[(9H-Fluoren-9-ylmethoxy)carbonyl]glycyl-glycine;N-9-Fluorenylmethoxycarbonylglycylglycine;2-(2-(((9H-fluoren-9-yl)methoxy)carbonylamino)acetamido)acetic acid;REF DUPL: Fmoc-Gly-Gly-OH;FMoc-Gly-Gly;FMoc-Gly4
• CAS NO: 35665-38-4
• Molecular Formula: C₁₉H₁₈N₂O₅
• Molecular Weight: 354.36
• EINECS: 1533716-785-6
• Product Categories: Amino Acid Derivatives
• Mol File: 35665-38-4.mol

Chemical Properties

• Melting Point: 176-177 °C
• Boiling Point: 684.086 °C at 760 mmHg
• Flash Point: 367.522 °C
• Appearance: White/Powder
• Density: 1.338 g/cm³
• Vapor Pressure: 1.19E-19mmHg at 25°C
• Refractive Index: 1.613
• Storage Temp.: -15°C
• PKA: 3.39±0.10(Predicted)
• CAS DataBase Reference: Fmoc-Gly-Gly-OH(CAS DataBase Reference)
• NIST Chemistry Reference: Fmoc-Gly-Gly-OH(35665-38-4)
• EPA Substance Registry System: Fmoc-Gly-Gly-OH(35665-38-4)

Safety Data

• Hazardous Substances Data: 35665-38-4(Hazardous Substances Data)

Usage

Uses

Used in Peptide Synthesis:
Fmoc-Gly-Gly-OH is used as a peptide linker for the synthesis of larger peptides and proteins. The Fmoc group provides a stable protecting group for the N-terminus, allowing for the stepwise addition of amino acids during solid-phase peptide synthesis. This method is widely employed in the production of therapeutic peptides, vaccines, and other bioactive molecules.
Used in Drug Delivery Systems:
In the pharmaceutical industry, Fmoc-Gly-Gly-OH is used as a component in the development of drug delivery systems. Its ability to form stable conjugates with various molecules, including drugs, targeting ligands, and imaging agents, makes it a valuable tool for enhancing the specificity, bioavailability, and overall efficacy of drug formulations.
Used in Bioconjugation and Molecular Probes:
Fmoc-Gly-Gly-OH is employed as a versatile building block in the creation of bioconjugates and molecular probes. Its reactivity and compatibility with various functional groups make it an ideal candidate for the development of novel imaging agents, biosensors, and other diagnostic tools.
Used in Research and Development:
In academic and industrial research settings, Fmoc-Gly-Gly-OH is used as a key component in the design and synthesis of novel bioactive molecules. Its ability to facilitate the formation of stable conjugates with a wide range of molecules makes it a valuable tool for exploring new chemical space and developing innovative therapeutic strategies.
Used in Chemical Synthesis:
Fmoc-Gly-Gly-OH is also utilized in various chemical synthesis processes, where its unique properties can be harnessed to create new compounds with potential applications in various industries, including pharmaceuticals, materials science, and agriculture.

InChI:InChI=1/C19H18N2O5/c22-17(20-10-18(23)24)9-21-19(25)26-11-16-14-7-3-1-5-12(14)13-6-2-4-8-15(13)16/h1-8,16H,9-11H2,(H,20,22)(H,21,25)(H,23,24)

Upstream product

• 35661-61-1 1-(N-fluoren-9-ylmethoxycarbonyl-glycyloxy)-piperidine 
• 56-40-6 glycine 
• 1370440-28-0 N-(((9H-fluoren-9-yl)methoxy)carbonyloxy)-2-amino-2-oxoacetimidoyl cyanide 
• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 556-50-3 glycylglycine 
• 1131148-55-4 1-[(9-fluorenylmethyloxycarbonyl)]benzotriazole 
• 29022-11-5 N-(fluoren-9-ylmethoxycarbonyl)glycine 
• 113484-74-5 2,5-dioxopyrrolidin-1-yl N-[(9H-fluoren-9-ylmethoxy)carbonyl]glycinate 

Downstream Products

• 790692-35-2 Ac-Gly-Gly-Phe-Cys(Et)-Ala-OH 

Relevant articles and documents

2D green SPPS: Green solvents for on-resin removal of acid sensitive protecting groups and lactamization

Aiming at greener synthesis of complex peptides we report that conventional one-dimensional (1D) green solid-phase peptide synthesis (SPPS) is elevated to a two-dimensional (2D) concept in which side chains in peptide resins are functionalized by suitable green tactics. Specifically, we disclose on-resin deblocking using trifluoroacetic acid (TFA)/triisopropylsilane (TIS) in EtOAc/MeCN used in a synthesis of a melanocortin receptor agonist comprising (i) 1D green SPPS (ii) 2D green SPPS by an on-resin TFA/TIS in EtOAc/MeCN deprotection of Lys(Mtt) and Asp(O-2-PhiPr) followed by a lactamization using PyBOP/DIEA in NBP/EtOAc (iii) TFA cleavage followed by green precipitation using 4-methyltetrahydropyran (MTHP)/n-heptane. A further application for our green deprotection protocol was found in peptide fragment cleavages off CTC resins.

Fmoc-Amox, A Suitable Reagent for the Introduction of Fmoc

Synthesis of most peptides is achieved using solid-phase peptide synthesis employing the Fmoc/tert-butyl strategy. However, the introduction of Fmoc in N-unprotected amino acids seems to be challenging due to the formation of dipeptides and sometimes tripeptides as impurities and β-alanyl impurities when Fmoc-OSu is used as well. Herein, we report an efficient and successful method using Fmoc-Amox, which is an oxime based derivative, toward the synthesis of Fmoc-glycine with no traces of side reactions. Fmoc-Amox is inexpensive, and Amox can be easily removed after the reaction, thus affording pure Fmoc-Gly-OH devoid of any detrimental impurities or contamination, mainly dipeptide or Amox itself, as shown by high-performance liquid chromatography and NMR, respectively.

Site-selective chemical cleavage of peptide bonds

Site-selective cleavage of extremely unreactive peptide bonds is a very important chemical modification that provides invaluable information regarding protein sequence, and it acts as a modulator of protein structure and function for therapeutic applications. For controlled and selective cleavage, a daunting task, chemical reagents must selectively recognize or bind to one or more amino acid residues in the peptide chain and selectively cleave a peptide bond. Building on this principle, we have developed an approach that utilizes a chemical reagent to selectively modify the serine residue in a peptide chain and leads to the cleavage of a peptide backbone at the N-terminus of the serine residue. After cleavage, modified residues can be converted back to the original fragments. This method exhibits broad substrate scope and selectively cleaves various bioactive peptides with post-translational modifications (e.g. N-acetylation and -methylation) and mutations (d- and β-amino acids), which are a known cause of age related diseases.

Penta-glycine copper(II) complexes in slightly alkaline solutions

The kinetics of the reaction of CuII(GGG), CuII(GGGGG) and CuII(GGGGS), where G = glycine and S = sarcosine, with 4-nitrophenyl-acetate were measured. The results point out that at pH 9.0 hydroxide is an axial, or equatori

Hydroxymethyl Salicylaldehyde Auxiliary for a Glycine-Dependent Amide-Forming Ligation

A new amide-forming ligation that requires a glycine or a primary amine at the linkage site is described herein. The distinguishing feature of this ligation is its reliance on an O-hydroxymethyl salicylaldehyde ester at the C-terminus which allows, via an N,O-acetal intermediate, the formation of a native peptide bond.

POLYCONJUGATES FOR DELIVERY OF RNAI TRIGGERS TO TUMOR CELLS IN VIVO

The present invention is directed compositions for delivery of RNA interference (RNAi) triggers to integrin positive tumor cells in vivo. The compositions comprise RGD ligand- targeted amphipathic membrane active polyamines reversibly modified with enzyme cleavable dipeptide-amidobenzyl-carbonate masking agents. Modification masks membrane activity of the polymer while reversibility provides physiological responsiveness. The reversibly modified polyamines (dynamic polyconjugate or conjugate) are further covalently linked to an RNAi trigger.

Benzotriazole reagents for the syntheses of Fmoc-, Boc-, and Alloc-protected amino acids

Stable Fmoc-, Boc-, and Alloc-benzotriazoles react with various amino acids including unprotected serine and glutamic acid, in the presence of triethylamine at 20° as reagents to introduce -amino protecting groups to afford Fmoc-, Boc-, and Alloc-protected amino acids (77-94%) free of dipeptide and tripeptide impurities. Fmoc-, and Alloc-Gly-Gly-OH dipeptides were prepared in 90% yields by N-acylation of glycylglycine with Fmoc- and Alloc-benzotriazoles in the presence of triethylamine. Synthesized N-protected amino acids were greater than 99% pure, analyzed by HPLC. Georg Thieme Verlag Stuttgart - New York.

Oxime carbonates: Novel reagents for the introduction of fmoc and alloc protecting groups, free of side reactions

Fmoc and Alloc protecting groups represent a consistent alternative to classical Boc protection in peptide chemistry. The former was established in the last decades as the α-amino protecting group of choice, whereas the latter allows a fully orthogonal protection strategy with Fmoc and Boc. Usually, the introduction of the Fmoc and Alloc moieties takes place through their halogenoformates, azides, or activated carbonates. This rather simple reaction is accompanied by several side reactions, specially the formation of Fmoc/Alloc dipeptides and even tripeptides. The present work describes new promising Fmoc/Alloc-oxime reagents, which are easy to prepare, stable, and highly reactive crystalline materials that afford almost: contaminant-free Fmoc/Alloc-amino acids in high yields by following a conventional procedure. Amongst the Fmoc-oxime derivatives, the N-hydroxypicolimmidoyl cyanide derivative (N-([(9H-fluoren-9-yl)methoxy]carbonyloxy}picolinimidoyl cyanide) gave the best results for the preparation of Fmoc-Gly-OH, which is the most predisposed to give side reactions. The same Alloc-oxime analogue afforded the preparation of Alloc-Gly-OH in good yield, purity, and extremely low dipeptide formation, as analyzed by reverse-phase HPLC and NMR spectroscopy.

Supramolecular Hydrogels Respond to Ligand-Receptor Interaction

N-(Fluorenyl-9-Methoxycarbonyl) dipeptides form supramolecular hydrogels via hydrogen bonding and hydrophobic interactions. These hydrogels respond to a ligand?receptor interaction as well as to thermal or pH perturbation and also exhibit chiral recognition. Copyright

Synthesis and application of a novel, crystalline phosphoramidite monomer with thiol terminus, suitable for the synthesis of DNA conjugates

A new, crystalline 5′-thiol modifier phosphoramidite monomer (3), suitable for DNA synthesis, has been prepared. This monomer has been built into an oligonucleotide using the standard protocol. After cleavage, purification and removal of the trityl group