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Determination of Peptide and Protein Disulfide Linkages by MALDI Mass Spectrometry

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Applications of MALDI-TOF Spectroscopy

Part of the book series: Topics in Current Chemistry ((TOPCURRCHEM,volume 331))

Abstract

The disulfide bond is one of the most common post-translational modifications in proteins, of which determination is essential to the comprehensive understanding of protein structures. Disulfide bond analysis has undergone great improvement due to the development of matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS), especially in terms of speed and sensitivity. In general, the characterization of disulfide-containing peptides is achieved by the reduction of disulfide bonds followed by alkylation. In this review we focus on the analysis of disulfide-containing proteins/peptides by some unique methods in MALDI MS. The MALDI in-source decay (ISD) of disulfide bonds and adducts of the matrix and sulfhydryl-containing peptide are discussed in detail. The mechanism of each method is discussed so as to help the reader gain greater insight into it, and examples of its application are also presented. The goal of this review is to provide an understanding of these techniques for analysis of disulfide-linked proteins/peptides in MALDI MS.

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Abbreviations

3-HCCA:

α-Cyano-3-hydroxycinnamic acid

APTA:

(3-Acrylamidopropyl)trimethylammonium chloride

ASA:

5-Aminosalicylic acid

BSA:

Bovine serum albumin

CA:

Caffeic acid

CAD:

Collision-activated dissociation

CDAP:

1-Cyano-4-(dimethylamino)pyridinium tetrafluoroborate

CHCA:

α-Cyano-4-hydroxycinnamic acid

CID:

Collision-induced dissociation

Cys:

Cysteine

Da:

Dalton

DAN:

1,5-Diaminonaphthalene

DHB:

2,5-Dihydroxybenzoic acid

DTT:

Dithiothreitol

ECD:

Electron capture dissociation

ESI:

Electrospray ionization

FA:

Ferulic acid

FAB:

Fast atom bombardment

FT-ICR:

Fourier transform ion cyclotron resonance

IAM:

Indoacetamide

ISD:

In-source decay

MALDI MS:

Matrix-assisted laser desorption/ionization mass spectrometry

ME:

β-Mercaptoethanol

NEM:

N-Ethylmaleimide

NMR:

Nuclear magnetic resonance

NSMA:

Negative signature mass algorithm

NTCB:

2-Nitro-5-thiocyanobenzoic acid

PSD:

Post-source decay

RNAseA:

Ribonuclease A

S/N:

Signal-to-noise ratio

SA:

Sinapinic acid

SDS:

Sodium dodecyl sulfate

THAP:

2, 4, 6-Trihydroxyacetophenone

TOF:

Time-of-flight

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Acknowledgments

This work was supported by China Postdoctoral Science Foundation funded project (No. 2012M511355), the National Natural Science Foundation of China (No. 21175127, 21175055), and Jilin Province Science and Technology Department (YYZX201131). We are very much indebted to all scientists quoted in the references.

Author information

Authors and Affiliations

  1. Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, 5625 Renmin Street, Changchun, 130022, China

    Hongmei Yang & Shuying Liu

  2. Central Laboratory, The Second Hospital of Jilin University, Changchun, 130041, China

    Ning Liu

  3. Changchun University of Chinese Medicine, Changchun, 130117, China

    Shuying Liu

Authors
  1. Hongmei Yang
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  2. Ning Liu
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  3. Shuying Liu
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Correspondence to Shuying Liu .

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Editors and Affiliations

  1. , Department of Chemistry, Hong Kong Baptist University, Ho Sin Hang Campus, Hong Kong, 000000000, China, People's Republic

    Zongwei Cai

  2. , Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, 000000000, China, People's Republic

    Shuying Liu

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© 2012 Springer-Verlag Berlin Heidelberg

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Yang, H., Liu, N., Liu, S. (2012). Determination of Peptide and Protein Disulfide Linkages by MALDI Mass Spectrometry. In: Cai, Z., Liu, S. (eds) Applications of MALDI-TOF Spectroscopy. Topics in Current Chemistry, vol 331. Springer, Berlin, Heidelberg. https://doi.org/10.1007/128_2012_384

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