The pH dependent mechanisms of non-enzymatic peptide bond cleavage reactions

2020 ◽  
Vol 22 (1) ◽  
pp. 107-113 ◽  
Author(s):  
Yi Sun ◽  
Moran Frenkel-Pinter ◽  
Charles L. Liotta ◽  
Martha A. Grover
Keyword(s):  
Bond Cleavage ◽  
Peptide Bond ◽  
Peptide Cleavage ◽  
Peptide Bond Cleavage ◽  
Ph Dependent ◽  
Cleavage Reactions

Peptide cleavage can occur through scission and backbiting, depending on the pH.

ChemInform Abstract: Unusual Peptide Bond Cleavage Reactions During Acidolytic Deprotection Reactions.

ChemInform ◽  
2010 ◽  
Vol 24 (28) ◽  
pp. no-no
Author(s):  
J. R. SPENCER ◽  
N. G. J. DELAET ◽  
A. TOY-PALMER ◽  
V. V. ANTONENKO ◽  
M. GOODMAN
Keyword(s):  
Bond Cleavage ◽  
Peptide Bond ◽  
Peptide Bond Cleavage ◽  
Cleavage Reactions

Facile peptide bond cleavage reactions

Peptides ◽  
1994 ◽  
pp. 211-214
Author(s):  
M. Goodman ◽  
J.R. Spencer ◽  
A. Toy-Palmer ◽  
J.X. Jiang ◽  
H.T. Li ◽  
...  
Keyword(s):  
Bond Cleavage ◽  
Peptide Bond ◽  
Peptide Bond Cleavage ◽  
Cleavage Reactions

scholarly journals Iodine induced alteration in immunological and biochemical properties of thyroglobulin.

1993 ◽  
Vol 40 (2) ◽  
pp. 237-240 ◽  
Author(s):  
A Gardas ◽  
H Domek
Keyword(s):  
Molecular Mass ◽  
Bond Cleavage ◽  
Coupling Reaction ◽  
Peptide Bond ◽  
Biochemical Properties ◽  
Disulphide Bridge ◽  
Peptide Bond Cleavage ◽  
Epitope Structure ◽  
Iodide Solution ◽  
Ph Dependent

The influence of iodine-iodide solution on the biochemical and immunological properties of human thyroglobulin (hTg) were studied. Human Tg preincubated with the iodine-iodide solution is split to small molecular mass fragments after disulphide bridge reduction with dithiothreitol. The peptide bond cleavage by iodine pretreatment and reduction is possibly linked with the coupling reaction of diiodotyrosyl residues. Pretreatment of hTg with iodine-iodide solution at 1-10 microM decreased the binding of autoantibodies to hTg. The iodine-iodide induced inactivation of hTg autoepitopes is pH dependent and is possibly caused by iodination of tyrosyl residues present in the epitope structure.

Unusual peptide bond cleavage reactions during acidolytic deprotection reactions

1993 ◽  
Vol 58 (6) ◽  
pp. 1635-1638 ◽  
Author(s):  
Jeffrey R. Spencer ◽  
Nancy G. J. Delaet ◽  
Anna Toy-Palmer ◽  
Valery V. Antonenko ◽  
Murray Goodman
Keyword(s):  
Bond Cleavage ◽  
Peptide Bond ◽  
Peptide Bond Cleavage ◽  
Cleavage Reactions

scholarly journals Serine protease dynamics revealed by NMR analysis of the thrombin-thrombomodulin complex

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Riley B. Peacock ◽  
Taylor McGrann ◽  
Marco Tonelli ◽  
Elizabeth A. Komives
Keyword(s):  
Active Site ◽  
Serine Proteases ◽  
Protein C ◽  
Catalytic Mechanism ◽  
Bond Cleavage ◽  
Peptide Bond ◽  
Peptide Bond Cleavage ◽  
Exchange Mass Spectrometry ◽  
Catalytically Active ◽  
Hydrogen Deuterium

AbstractSerine proteases catalyze a multi-step covalent catalytic mechanism of peptide bond cleavage. It has long been assumed that serine proteases including thrombin carry-out catalysis without significant conformational rearrangement of their stable two-β-barrel structure. We present nuclear magnetic resonance (NMR) and hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments on the thrombin-thrombomodulin (TM) complex. Thrombin promotes procoagulative fibrinogen cleavage when fibrinogen engages both the anion binding exosite 1 (ABE1) and the active site. It is thought that TM promotes cleavage of protein C by engaging ABE1 in a similar manner as fibrinogen. Thus, the thrombin-TM complex may represent the catalytically active, ABE1-engaged thrombin. Compared to apo- and active site inhibited-thrombin, we show that thrombin-TM has reduced μs-ms dynamics in the substrate binding (S1) pocket consistent with its known acceleration of protein C binding. Thrombin-TM has increased μs-ms dynamics in a β-strand connecting the TM binding site to the catalytic aspartate. Finally, thrombin-TM had doublet peaks indicative of dynamics that are slow on the NMR timescale in residues along the interface between the two β-barrels. Such dynamics may be responsible for facilitating the N-terminal product release and water molecule entry that are required for hydrolysis of the acyl-enzyme intermediate.

Activation of Bovine Factor V by Thrombin and A Protease From Russell's Viper Venom (RVV)

1979 ◽  
Author(s):  
M.J. Lindhout ◽  
C. M. Jackson
Keyword(s):  
Bond Cleavage ◽  
Peptide Bond ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Factor V ◽  
Peptide Bond Cleavage ◽  
Prothrombinase Complex ◽  
Factor Va ◽  
Activation Products ◽  
Ca Oxalate

In order to understand the function of activated factor V in the prothrombinase complex, we isolated the activation products obtained by action of thrombin and RVV-V on factor V and studied their functional properties. Factor V isolated from plasma by means of ion-exchange chromatography, a Ca-oxalate adsorption step and gelfiltration was homogenous in SDS-gelelectrophoresis (apparent MW 360,000, with and without reduction). Increase in factor V activity upon action by RVV-V is correlated with a single peptide bond cleavage, resulting in a 270,000 dalton and a 80,000 dalton component. Additional proteolysis of factor Va(RVV/V)’ by thrombin results in a further cleavage of the high MW component into peptides with MW's of 72,000, 94,000 and about 150,000 without a furth~r increase in factor V activity. Whereas none of the isolated peptides reveal factor Va activity, activity would be generated by a recombination in the presence of Ca2+ of the 94,000 MW or 270,000 MW component with the 80,000 component. Action of thrombin alone on factor V results in peptides of MW 72,000, 80,000, 94,000 and a peptide very rich in carbohydrate with an apparent MW of 150,000.

Demasking kinetics of peptide bond cleavage for whey protein isolate hydrolysed by Bacillus licheniformis protease

2016 ◽  
Vol 133 ◽  
pp. S426-S431 ◽  
Author(s):  
Mikhail M. Vorob’ev ◽  
Claire I. Butré ◽  
Stefano Sforza ◽  
Peter A. Wierenga ◽  
Harry Gruppen
Keyword(s):  
Whey Protein ◽  
Bacillus Licheniformis ◽  
Bond Cleavage ◽  
Peptide Bond ◽  
Whey Protein Isolate ◽  
Protein Isolate ◽  
Peptide Bond Cleavage ◽  
Kinetics Of
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