Method for improving mass spectrometry detection microorganism secondary crystal, and product

Abstract

The present invention provides a method for improving a microorganism sample secondary crystal. The method comprises: respectively adding 3-hydroxy-2-picolinic acid and a diammonium citrate solution in an acetonitrile aqueous solution to prepare a matrix solution, adding a specific proportion of a sample solution, and carrying out spotting crystallization on a chip. The present invention further provides a mass spectrometry correction method for improving the accuracy of biological target molecule detection mass spectrometry, wherein the mass spectrometry correction method comprises: spottinga matrix solution on a chip, crystallizing, spotting a microorganism sample on the chip, crystallizing, and bombarding the microorganism sample at a correction hole position through mass spectrometryso as to correct the mass spectrometry result of the sample to be detected, wherein a plurality of hydrophilic region positioning holes, outside-hydrophobic-hole regions, center correction holes, verification correction holes and spare correction holes are vertically arranged on the chip in a cross manner. The invention further provides a chip for the mass spectrometry correction and detection. According to the present invention, by improving the formula of the matrix solution, the primary crystal and the secondary crystal with good crystal morphology can be obtained; and with the correction method, the stable and accurate mass spectrometry detection result can be easily obtained.

Description

technical field [0001] The invention relates to a method for improving the accuracy rate of MALDI-TOF mass spectrometry detection by improving the crystallization and correction methods of biological samples, which can detect microorganisms by mass spectrometry and belongs to the technical field of mass spectrometry detection. Background technique [0002] Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) technology has become a classic technology in proteomics research. In the process of successful application of this technique, appropriate sample pretreatment methods play a primary and critical role. The accurate identification of biomacromolecules such as nucleic acids and proteins can be successfully achieved only by combining appropriate sample pretreatment methods with suitable organic matrices. The choice of matrix, solvents, salts (metal ions) and sample preparation methods are critical factors in the success or failure of M...

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Problems solved by technology

Since this method directly adds protein samples to the hydrophobic layer and purifies by adding excess matrix solution, although there is a certain purification effect objectively, it causes waste of protein samples

At the same time, if the manual operation is to place 0.2 μl of hydrophobic polymer solution in the small hole of each Kapton membrane, it is time-consuming, and the accuracy of the 0.2 μl solution is difficult to control, which will affect the hydrophobic uniformity of the surface of the small hole; if it is operated automatically, it needs to be configured The corresponding spotting equipment increases the cost and makes the preparation complicated, and is not suitable for the detection and application of trace protein samples that are not easy to prepare

[0010] Due to the previous research on the above-mentioned target plate, or there is no difference between hydrophilic and hydrophobic on the surface of the target plate (such as Chinese patent 200610023671.5), resulting in poor crystal morphology, or the formation of a coating with a difference between hydrophilic and hydrophobic, but the hydrophilic and hydrophobic water boundary cannot be reached. Micron precision or droplet contact angle is too small, but the preparation process is too complicated to save time and cost (such as Chinese patent 201410090967.3, patent 201110401165.6), or requires additional devices and detection software, or requires too many precious protein samples These all lead to low accuracy of mass spectrometry detection of sample peaks, low signal-to-noise ratio, and high baseline

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