What is Aspartimide formation?

Aspartimide formation 1,2 is caused by repeated exposure of aspartic acid containing sequences to bases like piperidine and can result ultimately in the generation of 9 different by-products (Figure 1)3–8.

What is the first step in the Merrifield peptide synthesis?

In the first method the N-t-butyloxycarbonyl (Boc) protected amino acid is attached to the solid phase via a linker moiety and the second protocol uses 9-fluorenylmethyloxycarbonyl (Fmoc) as the amino protecting group, which can be easily cleaved.

What is peptide bond formation?

A peptide bond also sometimes called eupeptide bond is a chemical bond that is formed by joining the carboxyl group of one amino acid to the amino group of another.

How is Aspartimide formation prevented?

One of the simplest strategies for limiting aspartimide formation is to change the Fmoc-removal conditions. Simply adding 0.1 M hydroxybenzotriazole (HOBt) to the piperidine solution has been shown to reduce aspartimide formation significantly.

What is Merrifield method?

Bruce Merrifield, involves attaching the C-terminus of the peptide chain to a polymeric solid, usually having the form of very small beads. Separation and purification is simply accomplished by filtering and washing the beads with appropriate solvents.

What is Merrifield solid phase peptide synthesis?

Merrifield solid phase peptide synthesis has been the principle research procedure used in the study of the chemistry and biological use of deamidation of asparaginyl and glutaminyl residues in peptides and proteins during the past 40 years.

How is peptide bond formed in translation?

During translation, peptide bonds are formed from the amino (N) to the carboxyl (C) terminus by removal of water (also referred to as dehydration or condensation) and catalyzed by RNA (referred to as a ribozyme) that forms part of the ribosome.

Which one is the best method for the synthesis of a long peptide?

The fragment condensation method has been used for the synthesis of long peptides. In this case, short fragments of the required peptide are first synthesized, then coupled together to form a long peptide.

How do I remove tBu protecting group?

The tBu group is removed using TFMSA, mercury (II) acetate, or TFA/dimethylsulfoxide/anisole. Recently, trimethylsilylbromide (TMSBr)-thioanisole/TFA was reported to cleave the tBu protecting group.

What are the types of EDC?

There are three primary categories of EDC software users: sites, sponsors, and CROs: Sites – A site refers to the entity that coordinates and collects data from the clinical trial patients, or subjects; usually a hospital or clinic.