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G. McCombie and R. Knochenmuss, “Small-Molecule MALDI using the Matrix Suppression Effect to Reduce or Eliminate Matrix Background Interferences,” Analytical Chemistry, Vol. 76, No. 17, 2004, pp. 4990-4997. doi:10.1021/ac049581r

has been cited by the following article:

• TITLE: Acylhydrazide and Isatin Schiff Bases as Alternate UV-Laser Desorption Ionization (LDI) Matrices for Low Molecular Weight (LMW) Peptides Analysis

  AUTHORS: Syed Ghulam Musharraf, Aisha Bibi, Najia Shahid, Muhammad Najam-ul-Haq, Momin Khan, Muhammad Taha, Uzma Rasool Mughal, Khalid Mohammed Khan

  KEYWORDS: MALDI-MS; LDI Matrix; Acylhydrazide Schiff Bases; Bis-Schiff Bases of Isatin; Schiff Bases of Isatin; Peptides

  JOURNAL NAME: American Journal of Analytical Chemistry, Vol.3 No.12, December 25, 2012

  ABSTRACT: Matrix-assisted laser desorption/ionization (MALDI) is a preferred and widely used mass spectrometric technique for the analysis of macromolecules. Limited UV-LDI matrices are available for the analysis of biomolecules due to the restricted structural features to serve in the laser desorption/ionization mechanism with a problem of background signals appearing in the low mass region. This paper describes the application of Schiff base derivatives of acylhydrazide and isatin as alternate UV-LDI matrices for the analysis of peptides with significantly low background signals. Thirty one compounds have been successfully employed as matrices for the analysis of low molecular weight (LMW) peptides (α-Cyano-4-hydroxycinnamic acid (HCCA), a preferred choice for peptide analysis.