Protein cleavage by transition metal complexes bearing amino acid substituents

Buranaprapuk, Apinya; Leach, Stephen P.; Kumar, Challa V.; Bocarsly, Jeffrey R.

doi:10.1016/s0167-4838(98)00145-9

Cited by 32 publications

(27 citation statements)

References 16 publications

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“…Early studies in the area of metal-promoted peptide cleavage employed metal complexes in combination with oxidoreductive additives to achieve either oxidative (68)(69)(70)(71)(72)(73)(74)(75)(76)(77)(78)(79)(80)(81)(82) Metal complexes [e.g., a Cu(I) complex of 1,10-phenanthroline (phen) or and Fe(II) complex of ethylenediaminetetraacetato (edta, ligand)] conjugated to deoxyribonucleic acid (DNA) binding ligands oxidatively cleave nucleic acids in the presence of redox additives (84,85). The redox chemistry of those coordination complexes is related to the oxidative cleavage of polypeptide backbones of proteins.…”

Section: A Agents For Oxidative Cleavage Of Proteinsmentioning

confidence: 99%

“…For example, [Cu(phen) 2 ] þ was exploited in the structural analysis of Escherichia coli lactose permease, a paradigm for membrane transport proteins (73). By the reaction of Y with a functional lactose permease mutant, phen was covalently linked to a single cysteine residue situated within one of the 12 membrane-spanning a-helices of the protein.…”

Section: A Agents For Oxidative Cleavage Of Proteinsmentioning

confidence: 99%

“…Characterization of protein fragments by N-terminal sequencing and MALDI-TOF MS identified the cleavage sites as Leu(89)-Ala (90) and Leu(72)-Gly (73) for Co (III) BU and Leu(89)-Ala(90) for Co (III) BV and Co (III) BW.…”

Section: Bw Bx Bvmentioning

confidence: 99%

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Peptide‐ or Protein‐Cleaving Agents Based on Metal Complexes

Chei¹,

Suh²

2007

Progress in Inorganic Chemistry

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Section: A Agents For Oxidative Cleavage Of Proteinsmentioning

confidence: 99%

Section: A Agents For Oxidative Cleavage Of Proteinsmentioning

confidence: 99%

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Peptide‐ or Protein‐Cleaving Agents Based on Metal Complexes

Chei¹,

Suh²

2007

Progress in Inorganic Chemistry

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“…Metal ions and complexes are used to effect cleavage of the polypeptide backbone under nondenaturing conditions of temperature and pH [34][35][36]41,[44][45][46][47][48][49][50][51][52]. Because mild conditions can be employed, these reagents show great promise for use in the analysis of protein solution structure, in protein engineering (e.g., the generation of semi-synthetic proteins, the proteolytic cleavage of bioengineered fusion proteins), and in therapeutics.…”

mentioning

confidence: 99%

Major Advances in the Hydrolysis of Peptides and Proteins by Metal Ions and Complexes

Grant¹,

Kassai

2006

COC

116

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Metal ions and complexes that hydrolyze peptides and proteins have become increasingly important in recent years. These reagents have shown great promise for use in a variety of applications including protein sequencing and proteomics. When metal-assisted hydrolytic cleavage is accomplished under nondenaturing conditions of temperature and pH, their use can be extended to include the study of protein function and solution structure, the generation of semisynthetic proteins, the proteolytic cleavage of bioengineered fusion proteins, and therapeutics. Yet, because of the extreme stability of the peptide amide bond, hydrolytically active metals are limited in number and there is now great interest in the development of new, more efficient reagents. In this review, we provide a description of relevant, early work with metal ions and complexes that have been used to hydrolyze unactivated peptide amide bonds in peptides and proteins. More importantly, we present an overview of recent contributions that have been made toward the development of synthetic metalloproteases that catalyze hydrolysis under near physiological conditions of temperature and pH.Dedicated to Professor Koji Nakanishi on the occasion of his 80 th birthday.

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“…The band corresponding to the full length of BSA disappeared almost completely after 36 hr. Although it was much slower than nature enzymes, the cleavage rate was on the same level to other kinds of chemical artificial proteases [7][8][9].…”

Section: Time Course Of the Extent Of Cleavagementioning

confidence: 99%

Cleavage of BSA by a dipeptide seryl-histidine

et al. 2000

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SummaryA dipeptide seryl-histidine (Set-His) was found to have the protein cleavage activity. BSA was cleaved into smear at around pH 5.0-6.0, with a half-life around 15 hr at 60 ~ Phosphate could accelerate the reaction. This is a brand new protein cleavage system. Since Ser and His are well-known catalytic residues at the active sites of many serine proteases, this results might provide clues to the possible roles of short oligopeptides in the origins of modern enzymes.

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Protein cleavage by transition metal complexes bearing amino acid substituents

Cited by 32 publications

References 16 publications

Peptide‐ or Protein‐Cleaving Agents Based on Metal Complexes

Peptide‐ or Protein‐Cleaving Agents Based on Metal Complexes

Major Advances in the Hydrolysis of Peptides and Proteins by Metal Ions and Complexes

Cleavage of BSA by a dipeptide seryl-histidine

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