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Title: Mechanism and applicability of hydrolysis of peptides and proteins utilizing Pt(II) complexes

Technical Report ·
DOI:https://doi.org/10.2172/6812379· OSTI ID:6812379

The hydrolysis of amino acid esters and amides has been achieved by using organic reagents, strongly acidic and basic solutions, and transition metal complexes. However, enzymes have always been able to surpass these methods in terms of speed of the hydrolysis and the mild conditions necessary to observe hydrolysis. In order to understand how enzymes undergo their reactions with such remarkable speed and efficiency, researchers are studying and developing inorganic reagents which can facilitate the hydrolysis of peptide bonds. The treatment of the tripetide {gamma}-glutamyl-cyteinylglycine with one equivalent of PtCl{sub 4}{sup {minus}2} results in hydrolysis of the cysteinyl-glycine bond. The reaction is strongly dependent on the amount of chloride ion in solution and also shows a lesser dependence on ionic strength and pH. Hydrolysis is promoted through a chelate interaction of the platinum with the sulfur of cysteine and the carbonyl oxygen of the amide bond. The hydrolysis of proteins was then undertaken. Yeast cytochrome c and the subunits of hemoglobin were examined to determine if PtCl{sub 4}{sup {minus}2} or Pt(en)Cl{sub 2} could promote cleavage of the peptide bond next to a cysteine residue. It appears that hydrolysis of the peptide bond to the right of the cysteinly side chain has been realized. 51 refs., 12 figs., 12 tabs.

Research Organization:
Ames Lab., Ames, IA (United States)
Sponsoring Organization:
DOE/ER
DOE Contract Number:
W-7405-ENG-82
OSTI ID:
6812379
Report Number(s):
IS-T-1468; ON: DE90012448; TRN: 90-021738
Resource Relation:
Other Information: Thesis (M.S.)
Country of Publication:
United States
Language:
English