In the last century, small-molecule natural products were the main inspiration for most drug
discovery programs based either on high-throughput screening (HTS) or rational design …

abstract Disulfide bridges play a crucial role in the folding and structural stabilization of
many important extracellular peptide and protein molecules, including hormones, enzymes …

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 …

Protein disulfide bonds link pairs of cysteine residues in polypeptide chains. Many of these
bonds serve a purely structural or energetic role, but a growing subset of cleavable disulfide …

The controlled formation of intramolecular disulfide bridges in peptides, while avoiding
unwanted oligomerization, is a significant challenge. Ellman's reagent, 5, 5 '-dithiobis (2 …

Bioactive peptides have potential as drug leads, but turning them into drugs is a challenge
because of their typically poor metabolic stability. Molecular grafting is one approach to …

Disulfide bonds are important structural moieties of proteins: they ensure proper folding,
provide stability, and ensure proper function. With the increasing use of proteins for …

Recently disulfide-rich head-to-tail cyclic peptides have attracted the interest of medicinal
chemists owing to their exceptional thermal, chemical and enzymatic stability brought about …

The goal of this review has been to present different chemical approaches for the formation
of disulfide bonds in synthetic peptides and small proteins. Three general types of …

Disulfide bridges play a crucial role in defining and rigidifying the three-dimensional
structure of peptides. However, disulfides are inherently unstable in reducing environments …