Abstract

The study of complexation of purine and pyrimidine derivatives with two kind of serum albumin using1H NMR and spectrofluorescence technique are performed in order to obtain model interactions nucleic acid bases–protein.The order of binding strength is as follows: 5mC > 5mU(T) > 3mU > U for pyrimidines and N6mAde > N6Ado > 1mAde > ATP > Ado > Ade for adenine derivatives.The effect of temperature on the hydrophobic interaction between the nitrogen bases and protein has been studied. The destabilization of protein structure causes loss of tertiary structural contacts, indicating that protein conformation is crucial for binding.

Highlights

  • The formation of protein–nucleic acid associations proceeds via hydrogen bonding

  • Sułkowska / Interaction of pyrimidine and purine bases with proteins human serum albumin (HSA) crystallized and lyophilised, fraction V were from WSiS – Lublin and Fluka, respectively

  • Methyl groups of nucleic acid bases and especially C5-methyl group in pyrimidine ring and N6 methyl group in adenine take an important role in interactions with protein

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Summary

Introduction

The formation of protein–nucleic acid associations proceeds via hydrogen bonding. It was safely assumed by spectroscopic studies [5] that this association occurs by the attachment of the amino acid side chains to the nucleic acid bases. It is of interest to assess the binding site of the nitrogen bases in protein and the strength of this binding. Such studies lead to better understanding of the structural basis for the sequence-specific recognition of deoxynucleic acid and the molecular basis of gene regulation. In this work we use 1H NMR and spectrofluorescence technique in order to obtain model interaction of rare nucleic acid bases and protein

Materials
Fluorescence measurements
Determination of the binding constant
Results and discussion
Quenching effect on protein fluorescence
Conclusions
Full Text
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