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- 蛋白药结构分析
- 2025年07月12日
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ProtTech Inc.
确定蛋白中二硫键的数目，位置及二硫键形成的比例。
ProtTech公司提供两种检测服务：
1). Analytical Disulfide Bond Mapping
Analytical disulfide bond mapping is aimed to determine the number, the position and ratio of disulfide bond linkage in a protein.
In this analysis, a protein samples is split into 2 fractions, one treated with Cysteine alkylation agent, the other is react with DTT to reduced all disulfide bond completely before reacting with Cys alkylation agent. Both fractions are digested with 2-3 proteolytic enzymes. The digestion products are then analyzed with an analytical HPLC system with a reverse-phase C18 column.
Disulfide bond-linked peptides are determined by our proprietary software based on the specific MS/MS features of the peptide, as well as the difference in the chromatogram between non-reduced and reduced sample. The ratio of S-S linked peptides as well as free Cys residues are determined based on the areas of corresponding peaks in the chromatogram.
We’ll report the ratio and each detected linkage of each system residues in the protein in a project report.
Due to use of analytical HPLC in this analysis, we require > 0.5mg protein with > 90% purity for S-S mapping. The service is used in the characterization of biologics samples at the development stage and the comparability study.
2). Micro Disulfide Bond Mapping
Micro disulfide bond mapping is often used for research stage protein samples that the disulfide linkage is unknown. The amount of a sample is often limited in a 10ug-100ug range, and the purity of the sample might be low. Therefore, it becomes necessary to use NanoLC-MS/MS system that is of more than thousands fold higher sensitivity in detection of disulfide bond linked peptides.
In micro disulfide mapping, a sample is split into 2 fractions, one with Cysteine alkylation only, and one with DTT reduction and alkylation. (Optionally, SDS-PAGE is used to further purify protein of interest.) Each fraction is then digested with 2-3 different proteolytic enzymes and digested samples were analyzed by NanoLC-ESI-MS/MS system. Our proprietary software is used to analysis MS and MS/MS data to specifically identify S-S bonds linked peptides and the determine the amino acid sequences of the linked peptides. The ratio of a peptide that does not form a disulfide bond can be determined semi-quantitatively based on EIC9 extracted ion current) of the peptides.
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文献和实验又称S － S 键。是 2 个 SH 基间被氧化而形成的 -CH2 — S — S — CH2 形式的硫原子间的键。在生物化学的领域中，通常系指在肽和蛋白质分子中的胱氨酸残基中的键。此键在蛋白质分子的立体结构形成上起着一定的重要作用。为了确定蛋白质的一级结构，首先必须将二硫键打开，使成为线状多肽链。为此，需要在 2- 巯 - 乙醇、二硫苏糖类、巯基乙酸等的硫化合物与尿素那样的变性剂同时存在下使之发生作用，使还原成 SH 基（为了防止再氧化通常用适当的 SH 试剂将该基团烷基
Characterization of Single-Domain Antibodies with an Engineered Disulfide Bond
. Specifically, we employ mass spectrometry fingerprinting analysis of VHH peptides to confirm the presence of the introduced disulfide bond, size exclusion chromatography, and surface plasmon resonance to examine the effects on aggregation state and target
Improvement of Single Domain Antibody Stability by Disulfide Bond Introduction
into the elucidation of rules to uniformly increase stability of antibodies. Recently, a novel intra-domain disulfide bond was independently discovered by two research groups, after either rational design or careful investigation of the naturally occurring camelid
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