Abstract
Experimental data on the separation of synthetic and natural peptides are presented as treated in terms of the separation model proposed by the authors, which allows for the chain connectivity of amino acid residues and the cooperative character of their interaction with the surface. It was shown that the model accurately predicts the separation of peptides with identical amino acid contents and different sequences of units in the chain. The differences in the sequence may be permutation of amino acid residues and the presence of terminal groups, amino acid isomers, or mirror sequences in the chain. The separation model was used to predict the retention times of peptides prepared via the enzymatic hydrolysis of E. coli proteins and bovine serum albumin with trypsin. It was shown that in general the model accurately explains the array of experimental data on the separation of such peptides, thus being the first successful attempt to relate the chain sequence to the retention volume.
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Original Russian Text © I.A. Tarasova, A.V. Gorshkov, V.V. Evreinov, K. Adams, R.A. Zubarev, M.V. Gorshkov, 2008, published in Vysokomolekulyarnye Soedineniya, Ser. A, 2008, Vol. 50, No. 3, pp. 479–493.
This work was supported by the Russian Academy of Sciences (Division of Chemistry and Materials Science) program “Design of High-performance Techniques for Chemical Analysis and Structure Study of Compounds and Materials;” the Russian Foundation for Basic Research, project no. 06-04-49632; and the INTAS Foundation, grant nos. 04-83-2643 and Genomics 05-10000004-7759.
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Tarasova, I.A., Gorshkov, A.V., Evreinov, V.V. et al. Applicability of the critical chromatography concept to proteomics problems: Experimental study of the dependence of peptide retention time on the sequence of amino acids in the chain. Polym. Sci. Ser. A 50, 309–321 (2008). https://doi.org/10.1134/S0965545X08030097
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DOI: https://doi.org/10.1134/S0965545X08030097