4.7 Article

O ? S Acyl Transfer Directing Human Sera Glycoprotein Immobilization for Breast Cancer Diagnosis

Journal

BIOCONJUGATE CHEMISTRY
Volume 34, Issue 4, Pages 664-672

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.bioconjchem.3c00017

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Breast cancer is a common malignancy with abnormal glycans. A synthetic boronic acid-disulfide (BASS) probe has been developed for glycoprotein recognition and labeling. The BASS-functionalized slide is a powerful platform for monitoring glycan pattern changes in human sera, particularly in breast cancer patients. This BASS-directed glycoprotein strategy shows promise for a rapid screening of clinical breast cancer samples and can be applied to other cancer prediagnoses.
Breast cancer (BC) is one of the most common malignancies in the world with aberrantly expressed glycans. The different types and stages still limit a comprehensive method in the prediagnosis of BC patients. In this research, a synthetic boronic acid-disulfide (BASS) probe has been developed for the two steps of O-* S-* N acyl transfer in glycoprotein recognition and labeling. The specificity and sensitivity of this method have been carefully studied in the case of immunoglobulin G, and the labeling efficiency was determined up to 60%. The BASS-functionalized slide is a powerful platform for monitoring the alteration of glycan patterns in human sera. Compared to the samples from healthy individuals, sera of BC patients gave specific patterns to eight lectins binding. The BASS-directed glycoprotein strategy promises a rapid sensing platform for a high-throughput screening of clinical BC samples and could be easily applied to other cancer prediagnoses.

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