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Global chain properties of an all l ‐α‐eicosapeptide with a secondary α‐helix and its all retro d ‐inverso‐α‐eicosapeptide estimated through the modeling of their CZE ‐determined electrophoretic mobilities
Author(s) -
Deiber Julio A.,
Piaggio Maria V.,
Peirotti Marta B.
Publication year - 2014
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201300395
Subject(s) - peptide , helix (gastropod) , chemistry , peptidomimetic , electrophoresis , chain (unit) , molecular dynamics , stereochemistry , biochemistry , computational chemistry , physics , biology , ecology , astronomy , snail
Several global chain properties of relatively long peptides composed of 20 amino acid residues are estimated through the modeling of their experimental effective electrophoretic mobilities determined by CZE for 2 < p H < 6. In this regard, an all l ‐α‐eicosapeptide, including a secondary α‐helix (Peptide 1) and its all retro d ‐inverso‐α‐eicosapeptide (Peptide 2), are considered. Despite Peptides 1 and 2 are isomeric chains, they do not present similar global conformations in the whole range of pH studied. These peptides may also differ in the quality of BGE components chain interactions depending on the p H value. Three Peptide 1 fragments (Peptides 3, 4, and 5) are also analyzed in this framework with the following purposes: (i) visualization of the effects of initial and final strands at each side of the α‐helix on the global chain conformations of Peptide 1 at different p H s and (ii) analysis of global chain conformations of Peptides 1 and 2, and Peptide 1 fragments in relation to their p I values. Also, the peptide maximum and minimum hydrations predicted by the model, compatible with experimental effective electrophoretic mobilities at different p H s, are quantified and discussed, and needs for further research concerning chain hydration are proposed. It is shown that CZE is a useful analytical tool for peptidomimetic designs and purposes.