The use of specially modified amino acids is available for a wide variety of peptide synthesis applications. These modified monomers are frequently extremely expensive and their implementation is limited by these costs.
Many naturally occurring peptides contain intradisulfide bridges, which play an important role in biological activities.
In peptide synthesis and peptide library synthesis, piperidine is a common reagent for Fmoc removal. However, piperidine is a controlled substance, which requires special handling.
Very fast synthesis times are achievable using optimized Fmoc conditions. Traditional peptide chemistry typically resorts to using extended reaction times to maintain synthesis yields, often resulting in deprotection times of 20-30 minutes and coupling times of an hour or more. It is accepted that speed is gained at the expense of purity.
Peptides are studied because of their range of biological activities in the body. As receptorbinding molecules, peptides have been investigated for therapeutic uses. Unfortunately, in the body peptides are easily broken down by proteases (enzymes that digest proteins and peptides) and have difficulty crossing cell membranes.
YIYGSFK is a substrate for the protein tyrosine kinase. Tyrosine kinase activity is increased in several human tumors, so the study of its substrates may lead to a greater understanding of cancer. In this application, a tyrosine kinase substrate was synthesized and modified with a biotinylated lysine and a racemic amino acid thioester on a Prelude peptide synthesizer using Boc chemistry.
The IntelliSynth™ UV-monitoring and Feedback Control System is a powerful tool that can be used to determine difficult cycles during a synthesis on the Tribute™ peptide synthesizer. It works by monitoring the extent of Fmoc removal during the deprotection reaction by measuring the concentration of removed Fmoc in the deprotection solution at 301 nm.
Biotinylation is the process of covalently binding biotin to a protein or other molecule. Due to the specificity and high binding affinity of biotin to the proteins avidin and streptavidin, biotinylation is commonly used in immunoanalytical techniques such as ELISA, ELISPOT and western blots.