Definition. FMOC chemistry describes a peptide synthesis strategy in which the 9-fluorenylmethoxycarbonyl group (Fmoc group) is used as a temporary protecting group for the N‐terminus. The Fmoc group is cleaved by secondary amines like piperidine.
How do I remove the Fmoc?
The Fmoc group is, in general, rapidly removed by primary (i.e., cyclohexylamine, ethanolamine) and some secondary (i.e., piperidine, piperazine) amines, and slowly removed by tertiary (i.e., triethylamine [Et3N], N, N-diisopropylethylamine [DIEA]) amines.
What is a scavenger in peptide synthesis?
Common scavengers include water (scavenges t-butyl cations), triisopropyl silane (TIS, scavenges trityl and Pbf cations), ethane dithiol (EDT, scavenges t-butyl cations, reduces oxidation of Cys/Met side chains), dioxa-1,8-octane-dithiol (DODT, scavenges t-butyl cations, suppresses oxidation of Cys/Met side chains),
Does TFA remove Fmoc?
All Answers (4) First remove Fmoc with a strong base (like TEA or piperidine in acetonitrile, chloroform, pyridine or other solvent, including DMF). Then remove BOC group by usual acidic treatment (TFA in dichloromethane or chloroform).
Is Fmoc stable in TFA?
It is stable in 50% TFA, but is removed under the standard peptide cleavage conditions (e.g. HF, TFMSOTf, TFSMA, HBr/AcOH). The Fmoc group is acid stable and Boc-Lys(Fmoc)-OH is used to prepare protected peptide fragments for fragment coupling.
How does TFA cleave peptides?
Under certain circumstances, TFA can cleave both at the linker-peptide bond and at the attachment point of the linker to the resin. In addition, the cleavage yield may be noticeably reduced due to a reaction between a Trp or Cys residue and the linker ion while still attached to the resin.
How do you protect Fmoc?
The Fmoc group is rapidly removed by primary bases as well as some secondary bases. Piperidine is usually preferred for Fmoc group removal as it forms a stable adduct with the dibenzofulvene byproduct, preventing it from reacting with the substrate.
Is Fmoc base-labile?
The fluorenylmethoxycarbonyl protecting group (Fmoc) is a base-labile protecting group used in organic synthesis.
Does TFA cleave Fmoc?
The side-chain protecting groups and linkers designed for fluorenylmethyloxycarbonyl (Fmoc) protocols are labile to trifluoroacetic acid (TFA). Under certain circumstances, TFA can cleave both at the linker-peptide bond and at the attachment point of the linker to the resin. Consequently, two events may occur.
What type of scavenger would you use for solid phase synthesis?
p-Methoxyphenol: A potent and effective scavenger for solid-phase peptide synthesis. J Pept Sci. 2020 Jun;26(6):e3251. doi: 10.1002/psc.
Which chemical is used as water scavenger in peptide synthesis?
Triisopropyl silane
What is BOC in peptide synthesis?
The use of the tert-butyloxycarbonyl (Boc) as the Nα-amino protecting group in peptide synthesis can be advantageous in several cases, such as synthesis of hydrophobic peptides and peptides containing ester and thioester moieties.