NMR analysis on the sialic acid‐binding mechanism of an R‐type lectin mutant by natural evolution‐mimicry

Abstract

A sialic acid-binding lectin (SRC) was created from the C-terminal domain of an R-type N-acetyl lactosamine-binding lectin (EW29Ch) by natural evolution-mimicry. Here, we clarified its sialic acid-binding mechanism using NMR spectroscopy. The NMR analysis showed differences between conformations of the 6 0 -sialyllactose-bound SRC in the solution state and that in the crystal state, and differences between the internal motion of the loop region in subdomain c in SRC and that of the corresponding region in EW29Ch. The NMR analysis thus provided useful information to explain the manner of binding to 6 0 -sialyllactose in solution, which the previous X-ray crystal structure analysis lacked.

Screening of a Sialyllactose-Specific Aptamer and Engineering a Pair of Recognition Elements with Unique Fluorescent Characteristics for Sensitive Detection of Sialyllactose

“…The content of SLs is an important nutritional index in infant formula milk powder. , Thus, the detection of SLs has wide applications in the evaluation of nutritional value in functional foods. So far, high-performance liquid chromatography (HPLC), mass spectrometric analyses, , proton nuclear magnetic resonance spectroscopy (NMR), and high-pH anion-exchange chromatography have been used for the identification and quantitative detection of SLs. Although these methods have been widely used in biomedical and food fields, they are time-consuming, costly, and cumbersome to operate.…”