Hydrolysis of insulin chain B using zirconium(iv) at neutral pH

Cepeda, Sarah S.; Grant, Kathryn B.

doi:10.1039/b715589a

Cited by 8 publications

(13 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Four cleavage sites were observed for reaction performed at 37 • C (Phe1-Val2, Gln4-His5, Leu6-Cys(SO 3 H)7, Gly8-Ser9) and five at 60 • C (additionally Gly20-Glu21). For another Zr(IV) compound, Zr(IV)-substituted 4,13-diaza-18-crown-6, 13 cleavage sites were detected after an 8 h incubation at pH 7.0 and 60 • C [82]. The major ones were: Gly8-Ser9, Gly20-Glu21, Ser9-His10, Cys(SO 3 H)7-Gly8, and Cys(SO 3 H)19-Gly20.…”

Section: Oxoanions and Pomsmentioning

confidence: 99%

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

Wezynfeld

Frączyk

Bal

2016

Coordination Chemistry Reviews

View full text Add to dashboard Cite

Section: Oxoanions and Pomsmentioning

confidence: 99%

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

Wezynfeld

Frączyk

Bal

2016

Coordination Chemistry Reviews

View full text Add to dashboard Cite

“…Up to now, hydrolysis of oxidized insulin chain B has been studied using a variety of metal salts and/or complexes based on Pd(II), Pt(II), Cu(II), Zn(II), and Zr(IV). 35,37,38,41,102 The resulting peptide fragments were also identified by various mass spectrometry based methods such as ESI-MS, HPLC-ESI-MS, MS/MS and MALDI-TOF. The hydrolytic reactions involving Pd(II), 102 Pt(II), 38 Cu(II) 38,102 and Zn(II) 37,41 were all conducted under harsh reaction conditions.…”

Section: Hydrolysis Of Oxidized Insulin Chain B Bymentioning

confidence: 99%

“…Nowadays, the use of metal-based complexes as artificial peptidases is on the rise. These transition metal and lanthanide based complexes have proven to be attractive candidates for hydrolyzing the unactivated peptide bond in dipeptides, [8][9][10][11][12][13][14][15][16][17][18][19][20][21] oligopeptides, 10,14,15,19,[22][23][24][25][26][27][28][29][30][31][32][33] polypeptides 28,[34][35][36][37][38][39][40][41] and proteins. 6,12,29,36,[42][43][44] However, metal complexes that efficiently catalyze peptide bond hydrolysis in a regioselective manner under mild reaction conditions still remain scarce.…”

Section: Introductionmentioning

confidence: 99%

Selective hydrolysis of oxidized insulin chain B by a Zr(iv)-substituted Wells–Dawson polyoxometalate

2015

View full text Add to dashboard Cite

We report for the first time on the selective hydrolysis of a polypeptide system by a metal-substituted polyoxometalate (POM). Oxidized insulin chain B, a 30 amino acid polypeptide, was selectively cleaved by the Zr(IV)-substituted Wells-Dawson POM, K15H[Zr(α2-P2W17O61)2]·25H2O, under physiological pH and temperature conditions in aqueous solution. HPLC-ESI-MS, LC-MS/MS, MALDI-TOF and MALDI-TOF MS/MS data indicate hydrolysis at the Phe1-Val2, Gln4-His5, Leu6-Cys(SO3H)7, and Gly8-Ser9 peptide bonds. The rate of oxidized insulin chain B hydrolysis (0.45 h(-1) at pH 7.0 and 60 °C) was calculated by fitting the integration values of its HPLC-UV signal to a first-order exponential decay function. (1)H NMR measurements show significant line broadening and shifting of the polypeptide resonances upon addition of the Zr(IV)-POM, indicating that interaction between the Zr(IV)-POM and the polypeptide takes place in solution. Circular dichroism (CD) measurements clearly prove that the flexible unfolded nature of the polypeptide was retained in the presence of the Zr(IV)-POM. The thermal stability of the Zr(IV)-POM in the presence of the polypeptide chain during the hydrolytic reaction was confirmed by (31)P NMR spectroscopy. Despite the highly negative charge of the Zr(IV)-POM, the mechanism of interaction appears to be dominated by a strong metal-directed binding between the positively charged Zr(IV) center and negatively charged amino acid side chains.

show abstract

“…At the optimum pH and temperature, k obs reached 3.21 Â 10 À2 h À1 , which is much faster than Zr 4þ and Ce 4þ complexes reported earlier. 28,29 Although the proteolytic potential of CMCR is weaker than trypsin hydrolysis at 32 C, pH ¼ 7.0, the simpler structure and lower cost may entitle more investigation and application in prospect.…”

Section: Stability Of Copper Ions On Cmcrmentioning

confidence: 99%

Synthesis and properties of an insoluble chitosan resin modified by azamacrocycle copper(II) complex for protein hydrolysis

Wang

Peng

et al. 2012

J of Applied Polymer Sci

View full text Add to dashboard Cite

We reported the synthesis process and the proteolytic ability of a novel crosslinked chitosan resin modified by azamacrocycle copper complex (CMCR). Characterization of CMCR showed that the Cu(II)Cyclen complex had successfully bound to the resin matrix covalently. Its proteolytic activity toward peptide bonds was evaluated by investigating the hydrolysis of bovine serum albumin in heterogeneous media. The maximum-observed pseudo-first-order rate constant (k obs ) was achieved under 60 C, pH 6.0, where protein was hydrolyzed into smaller peptides and amino acids confirmed by SDS-PAGE and ninhydrin reaction. The results indicated that the hydrolyzing efficiency delivered by CMCR was 4 Â 10 5 times higher than that of spontaneous hydrolysis. CMCR also featured a desirable stability for chelating Cu 2þ ions, which paved the way for its feasible recovery process and good reusability.

show abstract

Hydrolysis of insulin chain B using zirconium(iv) at neutral pH

Cited by 8 publications

References 30 publications

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

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

Selective hydrolysis of oxidized insulin chain B by a Zr(iv)-substituted Wells–Dawson polyoxometalate

Synthesis and properties of an insoluble chitosan resin modified by azamacrocycle copper(II) complex for protein hydrolysis

Contact Info

Product

Resources

About