Synthesis of single‐ and multiple‐stranded cystine‐rich peptides

Single Proline Residues can Dictate the Oxidative Folding Pathways of Cysteine-rich Peptides

“…In fact, from the large body of data collected over the years with cysteine-rich peptides and protein domains, a clear correlation between cysteine patterns and disulfide frameworks and thus overall folds has emerged, albeit with different origins and functions, and the poor sequence homology in the non-cysteine residues. [8][9][10][11][12][13][14] Also the PDB archive as of January 2006 does not contain any naturally occurring or spontaneously folding peptide or protein where this correlation is not observed, except for the cysteine-rich domains of minicollagen discussed here.…”

“…After 5 h digestion, two other species were detected whose intensities increase in timedependency. These exhibit the mass values of the fragments [10][11][12][13][14][15][16][17][18][19][20] and [21][22][23][24][25][26][27][28][29]. In addition, fragments were detected that correspond to the sequence portions [30][31][32][33] and [21][22][23][24][25][26][27][28][29], the latter one with an intramolecular peptide bond cleaved.…”

α-Selenoconotoxins, a New Class of Potent α7 Neuronal Nicotinic Receptor Antagonists

“…The use of such derivatives is also limited by their lack of commercial availability. Recently, it has been suggested that Boc chemistry can overcome the problems associated with the synthesis of selenocysteine-containing peptides (38). In contrast to Fmoc chemistry, Boc-SPPS has the advantage of clean and reliable N ␣ -Boc deprotection under acidic conditions, thus ensuring high yields during chain assembly (39) and avoiding excessive exposure to base, which compromises selenocysteine integrity (35).…”

A folded and functional synthetic PA1b: An interlocked entomotoxic miniprotein

“…The first one is based on the regioselective formation of disulfide bonds using an orthogonal protectiondeprotection scheme of cysteine-thiol. 27,28 Although this approach works very well for smaller peptides containing up to 6 cysteines, 29,30 it has not been applied so far for six-Cys containing interlocked peptides, like inhibitory cystineknots. In most cases, the formation of the cystine-knots 31,32 is a very efficient process when using the second approach consisting in direct oxidative folding, that is, the oxido-shuffling procedure in the presence of a redox system.…”