Protecting group chemistry for the cysteine thiol group has enabled a vast array of peptide
and protein chemistry over the last several decades. Increasingly sophisticated strategies for …

Synthetic organic chemistry is based on the concourse of reagents and catalysts to achieve
the clean formation of new bonds, and appropriate protecting groups are required to prevent …

Organic chemists working on the synthesis of natural products have long found a special
challenge in the preparation of peptides and proteins. However, more reliable, more efficient …

The concept of a glucose-responsive insulin (GRI) has been a recent objective of diabetes
technology. The idea behind the GRI is to create a therapeutic that modulates its potency …

The pancreatic peptide hormone insulin, first discovered exactly 100 years ago, is essential
for glycemic control and is used as a therapeutic for the treatment of type 1 and, increasingly …

Thiolated polymers are widely used in hydrogels for drug delivery, tissue engineering, and
biofabrication. The oxidation of thiols is spontaneous, resulting in the formation of disulfide …

Disulfide bonds play an important role in both proteins and peptides. They cause
conformational constraints and increase the stability of such molecules. In nature, disulfide …

Protecting group chemistry plays a pivotal role during peptide synthesis. For the synthesis of
cysteinyl peptides, this is more significant as cysteine (Cys) is involved in the formation of …

Reversible attachment of solubilizing tags to hydrophobic peptides to facilitate their
purification and ligation is an essential yet challenging task in chemical protein synthesis …

The disulfide bond plays an important role in biological systems. It defines global
conformation, and ultimately the biological activity and stability of the peptide or protein. It is …