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Electroactivity of Nonconjugated Proteins and Peptides. Towards Electroanalysis of All Proteins
Author(s) -
Paleček Emil,
Ostatná Veronika
Publication year - 2007
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/elan.200704033
Subject(s) - biomedicine , chemistry , electrochemistry , nucleic acid , tryptophan , tyrosine , combinatorial chemistry , proteomics , biochemistry , amino acid , nanotechnology , electrode , materials science , biology , bioinformatics , gene
Present proteomics and biomedicine require sensitive analytical methods for all proteins. Recent progress in electrochemical analysis of peptides and proteins based on their intrinsic electroactivity is reviewed. Tyrosine and/or tryptophan‐containing proteins are oxidizable at carbon electrodes. At mercury electrodes all peptides and proteins (about 13 peptides and >25 proteins were tested) produce chronopotentiometric peak H at nanomolar concentrations. This peak is sensitive to changes in protein structure. Microliter sample volumes are sufficient for the analysis. Electrochemical methods can be used in studies of nucleic acid‐protein interactions and can be applied in biomedicine. Examples of such applications in neurogenerative diseases and cancer are presented.