Influence of amino acids on the precipitation kinetics of calcium oxalate monohydrate

1993 ◽  
Vol 132 (1-2) ◽  
pp. 122-128 ◽  
Author(s):  
Lj. Komunjer ◽  
M. Marković ◽  
H. Füredi-Milhofer
2001 ◽  
Vol 101 (2) ◽  
pp. 159-168 ◽  
Author(s):  
David E. FLEMING ◽  
Wilhelm VAN BRONSWIJK ◽  
Rosemary Lyons RYALL

To assess the binding of individual amino acids to the principal calcium minerals found in human kidney stones, the adsorption of 20 amino acids on to calcium oxalate monohydrate, CaHPO4.2H2O, Ca3(PO4)2 and Ca5(PO4)3OH crystals was determined over the physiological urinary pH range (pH 5–8) in aqueous solutions. All amino acids adsorbed most strongly at pH 5, and this decreased in all cases as the pH was increased. The amino acids which adsorbed most strongly were aspartic acid, glutamic acid and γ-carboxyglutamic acid, with the last displaying the strongest affinity. All amino acids bound more avidly to calcium oxalate monohydrate than to any of the phosphate minerals. Adsorption on to CaHPO4.2H2O was generally higher than for Ca3(PO4)2 and Ca5(PO4)3OH, for which all amino acids, with the exception of γ-carboxyglutamic acid, had only a weak affinity. The binding affinity of these acids is thought to be due to their zwitterions being able to adopt conformations in which two carboxyl groups, and possibly the amino group, can interact with the mineral surface without further rotation. The strong binding affinity of di-and tri-carboxylic acids for calcium stone minerals indicates that proteins rich in these amino acids are more likely to play a functional role in stone pathogenesis than those possessing only a few such residues. These findings, as well as the preferential adsorption of the amino acids for calcium oxalate monohydrate rather than calcium phosphate minerals, have ramifications for research aimed at discovering the true role of proteins in stone formation and for potential application in the design of synthetic peptides for use in stone therapy.


2021 ◽  
Vol 28 ◽  
Author(s):  
Priyadarshini ◽  
Abhishek Negi ◽  
Chetna Faujdar ◽  
Lokesh Nigam ◽  
Naidu Subbarao

Background: Human serum albumin (HSA) is one of the most abundant proteins in the blood plasma, urine as well as in the organic matrix of renal calculi. Macromolecules present in the urine modulate kidney stone formation either by stimulating or inhibiting crystallization process. Objective: In the present study, effect of HSA protein on the growth of calcium oxalate monohydrate crystal (COM) was investigated. Methods: Crystal growth assay was used to measure oxalate depletion in the crystal seeded solution in the presence of HSA. HSA concentrations exhibiting effect on crystal growth were selected for FTIR and XRD analysis. In silico docking was performed on seven different binding sites of HSA. Results: Albumin is playing dual role in growth of calcium oxalate crystallization. FTIR and XRD studies further revealed HSA exerted strain over crystal thus affecting its structure by interacting with amino acids of its pocket 1. Docking results indicate that out of 7 binding pocket in protein, calcium oxalate interacts with Arg-186 and Lys-190 amino acids of pocket 1. Conclusion: Our study confirms the role of HSA in calcium oxalate crystallization where acidic amino acids arginine and lysine are binding with COM crystals, revealing molecular interaction of macromolecule and crystal in urolithiasis.


2014 ◽  
Vol 55 (7) ◽  
pp. 1356-1370 ◽  
Author(s):  
O. A. Golovanova ◽  
Yu. O. Punin ◽  
A. R. Izatulina ◽  
V. V. Korol’kov

1983 ◽  
Vol 64 (2) ◽  
pp. 306-315 ◽  
Author(s):  
Leo J.M.J. Blomen ◽  
Eric J. Will ◽  
Olav L.M. Bijvoet ◽  
Hanneke van der Linden

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