Metal complexes as artificial proteases in proteomics: A palladium(II) complex cleaves various proteins in solutions containing detergents

Metal assisted peptide bond hydrolysis: Chemistry, biotechnology and toxicological implications

“…Pd(II) complexes performed the cleavage of cytochrome c, Mb, ubiquitin, ␤-casein and BSA [47,83,84]. Cytochrome c was cleaved at sites His18↓Thr19, Gly24↓Lys25-His26, Asn31↓Leu32 His33, Thr63↓Leu64-Met65, Thr78↓Lys79-Met80 (metal anchoring residues in italics, hydrolysis sited marked with ↓) [47,85].…”

“…Cytochrome c was cleaved at sites His18↓Thr19, Gly24↓Lys25-His26, Asn31↓Leu32 His33, Thr63↓Leu64-Met65, Thr78↓Lys79-Met80 (metal anchoring residues in italics, hydrolysis sited marked with ↓) [47,85]. Ubiquitin was susceptible to hydrolysis by Pd(II) at site Thr66↓Leu67-His68 with and without the presence of a detergent (CHAPS or and at several other sites in the presence of CHAPS or Zwittergent 3-14 [47,84]. Mb was cleaved by Pd(II) at 13 sites, in the vicinity of methionine, histidine, and arginine residues [83].…”

“…Mb was cleaved by Pd(II) at 13 sites, in the vicinity of methionine, histidine, and arginine residues [83]. ␤-casein, a 224-amino-acid protein had 24 scissile peptide bonds [84]. BSA (607 amino acids) was cleaved at 80 sites in the presence of CHAPS and Zwittergent 3-14 [84].…”

“…␤-casein, a 224-amino-acid protein had 24 scissile peptide bonds [84]. BSA (607 amino acids) was cleaved at 80 sites in the presence of CHAPS and Zwittergent 3-14 [84].…”

“…Low sequence specificity, determined by single amino acid residues, primarily His and Met, providing the anchors for the formation of acid stable Pd(II) and Pt(II) complexes, was proposed to be turned into an advantage, as providing a facile tool for protein fragmentation in mass spectrometry procedures of protein identification [84]. Among several fragmentation protocols used in these procedures, the most popular one is provided by trypsin, which cleaves peptide bonds flanked by Lys or Arg residues [138].…”