Interaction of oligonucleotides with barrier fluid proteins.
Affinity modification of proteins was used to study their interaction with oligonucleotides barrier fluids. Several proteins of saliva and tears were shown to undergo affinity modification during incubation with an alkylating derivative of deoxyribooligonucleotides. In tears, such proteins were lactoferrin, immunoglobin G and lysozyme; in saliva, immunoglobulin A and lysozyme. The data showed that the affinity for oligonucleotides decrease in the order lactoferrin > lysozyme > immunoglobulin A > immunoglobulin G. The binding of reactive oligonucleotide derivatives with the proteins was competitively inhibited by polyanions, such as oligonucleotides of various nucleotide compositions, single-stranded and double-stranded DNA, heparin, and dextran sulfate. Interactions between oligonucleotides and proteins can strongly affect the metabolism of oligonucleotides and their ability to permeate biological barriers.