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Peptides, while exhibiting potential for unique specificity and affinity, still suffer from stability issues when introduced to a biological system. One strategy to overcome these stability issues is ...

Peptides, by nature, are composed of amino acids with potentially ionizable chemical moieties. The ionization state of any of these moieties can significantly impact the peptide’s chromatographic beha...

As the complexity of peptides continues to grow, so does the use of amino acids with side chain protecting groups that can be selectively removed, leaving the peptide on resin and the remaining side c...

Orthogonal amino acid protecting groups effectively expand the chemical tool kit available to peptide chemists allowing for synthesis of much more complex molecules. Often times, orthogonal protecting...

Disulphide rich peptides are being identified in species of both plants and animals at increasing rates. As new molecules are discovered and disulphide bonding patterns characterized, the need for sim...

In a previous post, I did some work evaluating the efficiency of alloc removal with tetrakis palladium using microwave assistance and atmospheric conditions, which worked beautifully.

Hydrocarbon stapling as a strategy to stabilize secondary structures of peptides, while introduced by Miller, Blackwell and Grubbs in the mid 1990s, really grew to the forefront with seminal work by S...

Orthogonal side chain protecting groups, particularly for Fmoc-based solid phase peptide synthesis, are growing not only in diversity, but also in popularity. These protecting groups enable post-synth...

Disulphide rich peptides have gained significant attention recently due to their incredible biological stability and tolerance to epitope grafting. This class of peptides is often folded in solution, ...

When it comes to synthesizing a peptide, the first thing that comes to mind is the number of stoichiometric equivalents to use. Sometimes that number is as few as 1.5, sometimes it’s as high as 20! Bu...