Metallionenkatalytische Zerlegung der (CONH)‐Bindung in Peptiden und N‐Acetyl‐Aminosäuren

Bamann, Eugen; Haas, Johann Georg; Trapmann, Heinz

doi:10.1002/ardp.19612940909

Cited by 19 publications

(15 citation statements)

References 40 publications

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“…At pH values greater than 5.0, low levels of peptide hydrolysis could be detected after 72 h of treatment at 75 °C. Similar results were obtained by Bamann and coworkers, who in 1961 showed that Co II ions could be used to hydrolyze GlyLeu at detectable levels after 24 h at pH 8.6 and 70 °C [66]. Yet Co II , which is kinetically labile, is readily oxidized by atmospheric oxygen to inert Co III .…”

Section: Cobalt Ions and Complexessupporting

confidence: 82%

“…In this study, the dipeptide Gly-Leu was hydrolyzed at low levels after treatment with Zn II for 24 h at pH 8.6 and 70°C [66]. More recently, Yashiro's group reacted ZnCl 2 with an extensive series of dipeptides [84].…”

Section: Divalent Zincmentioning

confidence: 97%

“…One of the earliest examples of Zn II -assisted peptide hydrolysis was published by Bamann and coworkers in 1961 [66]. In this study, the dipeptide Gly-Leu was hydrolyzed at low levels after treatment with Zn II for 24 h at pH 8.6 and 70°C [66].…”

Section: Divalent Zincmentioning

confidence: 97%

“…In the case of Cu II , Co III , Ni II , Pd II , and Pt II , intact proteins have also been cleaved [32][33][34]36,49,50,74,75,82,86,[89][90][91][92][93][94][95][96][97][98]. Although hydrolysis is sometimes accomplished at ~pH 7.0 and 37 °C [34][35][36]41,[47][48][49][50][51][52], either extreme pH, and/or elevated temperatures are ocassionally employed [32,33,[63][64][65][66][67][68][69][70][71][72][73][74][75][76][77][78][82][83]…”

mentioning

confidence: 97%

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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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Section: Cobalt Ions and Complexessupporting

confidence: 82%

Section: Divalent Zincmentioning

confidence: 97%

Section: Divalent Zincmentioning

confidence: 97%

mentioning

confidence: 97%

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

Grant¹,

Kassai

2006

COC

116

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“…Westheimer and Trapmann groups showed that Co(II), Cu(II) and Ni(II) ions are able to cleave Phe-Gly-NH 2 and Gly-Leu dipeptides [33,34]. No mechanistic concepts were proposed for these reactions that were performed at 75 • C, a temperature sufficient for partial hydrolysis of dipeptides in the absence of metal ions.…”

Section: Various Metal Complexesmentioning

confidence: 99%

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

Wezynfeld

Frączyk

Bal

2016

Coordination Chemistry Reviews

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Die durch Zusatz von Metallsalzen beschleunigte Lactamisierung der Glutaminsäure

Bamman

Münstermann

1965

Archiv der Pharmazie

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In Anwesenheit bestimmter Metallsalze, vor allen von Ionen der Elemente der 4. Nebengruppe sowie der Lanthaniden, erfährt die Lactamisierung der Glutaminsäure im schwach saueren bis schwach alkalischen Bereich bei mittleren Temperaturen (70°) eine erhebliche Beschleunigung, wobei das Optimum der Reaktion im schwach alkalischen Medium liegt. Ohne zusätzliche Katalysatoren geht die Pyrrolidoncarbonsäure‐Bildung in beachtenswertem Umfang nur im stärker saueren und im stärker alkalischen Gebiet vor sich; im pH‐Bereich von 6 bis 8 ist sie kaum nachweisbar. Die metallionenkatalytische Reaktion wird in ihrem Mechanismus aufgeklärt.

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Metallionenkatalytische Zerlegung der (CONH)‐Bindung in Peptiden und N‐Acetyl‐Aminosäuren

Cited by 19 publications

References 40 publications

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

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

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

Die durch Zusatz von Metallsalzen beschleunigte Lactamisierung der Glutaminsäure

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