Immuno-Affinity Study of Oxidative Tyrosine Containing Peptides

Protein tyrosine oxidations is thought to occur predominantly in an increasing number of pathophysiological conditions, hence the specific identification of tyrosine modification in native biological sample is highly desirable. Although different analytical techniques for identifying and detecting n...

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Bibliographic Details
Published in:International journal of peptide research and therapeutics 2022, Vol.28 (1), Article 41
Main Authors: Darie-Ion, Laura, Neamtu, Andrei, Iliescu, Radu, Petre, Brindusa Alina
Format: Article
Language:English
Subjects:
Affinity
Animal Anatomy
Antibodies
Biochemistry
Biomedical and Life Sciences
Biosensors
Histology
Life Sciences
Molecular Medicine
Molecular modelling
Morphology
Nitration
Nitrotyrosine
Peptides
Pharmaceutical Sciences/Technology
Pharmacology/Toxicology
Polymer Sciences
Tyrosine
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Summary:Protein tyrosine oxidations is thought to occur predominantly in an increasing number of pathophysiological conditions, hence the specific identification of tyrosine modification in native biological sample is highly desirable. Although different analytical techniques for identifying and detecting nitro-tyrosine modification in proteins have been employed their wide area of sensitivities and specificities, were not overcoming the risk of obtaining both, false positive and false negative identifications. The detection of tyrosine nitration has been mostly derived from the use of anti-3-nitrotyrosine (3-NT) antibodies with the risk of facing not specific results and cross reactivity with similar oxidative species or tyrosine embedded structural motifs. Therefore, in this study, synthetic model peptides containing nitro-Tyr, hydroxy-Tyr and unmodified Tyr residues were used to characterize positive versus false-positive affinity binding to anti 3-NT antibodies. The affinity interactions were measured by using surface-acoustic wave biosensor technology, a well-established tool for the detection and quantification of diverse biomolecular interactions. Our results indicate that anti 3-NT antibodies exhibit high affinity binding to both, nitro and hydroxy-Tyr containing peptides, crucial observation for all immunological methods. Moreover, molecular modeling studies revealed that the posttranslational modified tyrosine residues have also the highest solvent accessible surface areas. Our findings suggest that oxidative modifications in biological samples by endogenous oxidative reactive species require specific structural sequence motifs and close proximity to their cellular generation.
ISSN:1573-3149
1573-3904
DOI:10.1007/s10989-021-10329-2