116747-54-7

Basic information

• Product Name: FMOC-ALA-GLY-OH
• Synonyms: FMOC-ALA-GLY-OH;FMOC-L-ALANYL-GLYCINE;(S)-2-(2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)propanamido)acetic acid;(9H-Fluoren-9-yl)MethOxy]Carbonyl Ala-Gly-OH
• CAS NO: 116747-54-7
• Molecular Formula: C₂₀H₂₀N₂O₅
• Molecular Weight: 368.38
• Mol File: 116747-54-7.mol
• Article Data: 10

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: FMOC-ALA-GLY-OH(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-ALA-GLY-OH(116747-54-7)
• EPA Substance Registry System: FMOC-ALA-GLY-OH(116747-54-7)

Safety Data

• Hazardous Substances Data: 116747-54-7(Hazardous Substances Data)

Usage

General Description

FMOC-ALA-GLY-OH is a chemical compound consisting of three amino acids: FMOC, alanine (ALA), and glycine (GLY). FMOC is a protecting group commonly used in the synthesis of peptide chains, while ALA and GLY are both natural amino acids found in proteins. When combined, these amino acids form a peptide with the potential to be used in research, pharmaceuticals, or other applications. The compound is often used in the field of biochemistry and organic chemistry to study peptide synthesis and structure.

Upstream product

• 139928-78-2 benzyl (((9H-fluoren-9-yl)methoxy)carbonyl)-L-alanylglycinate 
• 131124-64-6 Fmoc-Ala-benzotriazolyl ester 
• 56-40-6 glycine 
• 35661-39-3 N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 
• 931120-55-7 Kb-Gly-Ala-Fmoc 
• 29022-11-5 N-(fluoren-9-ylmethoxycarbonyl)glycine 
• 912557-11-0 Fmoc-Ala-Gly-OtBu 
• 103321-50-2 9H-fluoren-9-ylmethyl [(1S)-2-chloro-1-methyl-oxoethyl]carbamate 
• 73724-40-0 (S)-2,5-dioxopyrrolidin-1-yl 2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)propanoate 

Relevant articles and documents

NEODEGRADER CONJUGATES

The present disclosure provides neoDegraders and neoDegraders conjugated to binding moieties. Also provided are compositions comprising the conjugates. The compounds and compositions are useful for treating a disease or condition, e.g., cancer, in a subject in need thereof.

A catalytic one-step synthesis of peptide thioacids: the synthesis of leuprorelin via iterative peptide-fragment coupling reactions

A catalytic one-step synthesis of peptide thioacids was developed. The oxygen-sulfur atom exchange reaction converted the carboxy group at the C-terminus of the peptides into a thiocarboxy group with suppressed epimerization. This method was successfully applied to the synthesis of the peptide drug leuprorelin via an iterative fragment-coupling protocol.

Characterization of Nα-Fmoc-protected dipeptide isomers by electrospray ionization tandem mass spectrometry (ESI-MSn): Effect of protecting group on fragmentation of dipeptides

A series of positional isomeric pairs of Fmoc-protected dipeptides, Fmoc-Gly-Xxx-OY/Fmoc-Xxx-Gly-OY (Xxx = Ala, Val, Leu, Phe) and Fmoc-Ala-Xxx-OY/Fmoc-Xxx-Ala-OY (Xxx = Leu, Phe) (Fmoc = [(9-fluorenylmethyl) oxy]carbonyl) and Y = CH3/H), have been characterized and differentiated by both positive and negative ion electrospray ionization ion-trap tandem mass spectrometry (ESI-IT-MSn). In contrast to the behavior of reported unprotected dipeptide isomers which mainly produce y 1+ and/or a1+ ions, the protonated Fmoc-Xxx-Gly-OY, Fmoc-Ala-Xxx-OY and Fmoc-Xxx-Ala-OY yield significant b 1+ ions. These ions are formed, presumably with stable protonated aziridinone structures. However, the peptides with Gly- at the N-terminus do not form b1+ ions. The [M + H]+ ions of all the peptides undergo a McLafferty-type rearrangement followed by loss of CO2 to form [M + H-Fmoc + H]+. The MS3 collision-induced dissociation (CID) of these ions helps distinguish the pairs of isomeric dipeptides studied in this work. Further, negative ion MS 3 CID has also been found to be useful for differentiating these isomeric peptide acids. The MS3 of [M-H-Fmoc + H]- of isomeric peptide acids produce c1-, z1 - and y1- ions. Thus the present study of Fmoc-protected peptides provides additional information on mass spectral characterization of the dipeptides and distinguishes the positional isomers. Copyright