Rapid Sequencing of Library-Derived Peptides by Partial Edman Degradation and Mass Spectrometry

2001 ◽  
Vol 3 (3) ◽  
pp. 251-254 ◽  
Author(s):  
Peng Wang ◽  
Gulnur Arabaci ◽  
Dehua Pei
Keyword(s):  
Mass Spectrometry ◽  
Edman Degradation ◽  
Partial Edman Degradation

scholarly journals High-Throughput Sequencing of Peptoids and Peptide−Peptoid Hybrids by Partial Edman Degradation and Mass Spectrometry

2009 ◽  
Vol 11 (2) ◽  
pp. 294-302 ◽  
Author(s):  
Amit Thakkar ◽  
Allison S. Cohen ◽  
Michael D. Connolly ◽  
Ronald N. Zuckermann ◽  
Dehua Pei
Keyword(s):  
Mass Spectrometry ◽  
High Throughput ◽  
High Throughput Sequencing ◽  
Edman Degradation ◽  
Partial Edman Degradation

Rapid primary structure determination of myoglobins by a complementary approach based on mass spectrometry and Edman degradation

2012 ◽  
Vol 133 (4) ◽  
pp. 1646-1652 ◽  
Author(s):  
Roberta Dosi ◽  
Annamaria Carusone ◽  
Angela Chambery ◽  
Valeria Severino ◽  
Augusto Parente ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Structure Determination ◽  
Primary Structure ◽  
Edman Degradation ◽  
Complementary Approach

Sequencing of Peptide Mixtures by Edman Degradation and Field-Desorption Mass Spectrometry

1980 ◽  
Vol 112 (2) ◽  
pp. 251-264 ◽  
Author(s):  
Yasutsugu SHIMONISHI ◽  
Yeong-Man HONG ◽  
Toyoko KITAGISHI ◽  
Takekiyo MATSUO ◽  
Hisashi MATSUDA ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Edman Degradation ◽  
Field Desorption ◽  
Desorption Mass Spectrometry ◽  
Peptide Mixtures ◽  
Field Desorption Mass Spectrometry

scholarly journals Inhibition of Staphylococcus aureus Cell Wall Biosynthesis by Desleucyl-Oritavancin: a Quantitative Peptidoglycan Composition Analysis by Mass Spectrometry

2017 ◽  
Vol 199 (15) ◽  
Author(s):  
James D. Chang ◽  
Erin E. Foster ◽  
Aanchal N. Thadani ◽  
Alejandro J. Ramirez ◽  
Sung Joon Kim
Keyword(s):  
Mass Spectrometry ◽  
Staphylococcus Aureus ◽  
Cell Wall ◽  
Binding Site ◽  
Mode Of Action ◽  
Composition Analysis ◽  
Edman Degradation ◽  
Glycopeptide Antibiotics ◽  
Content Type ◽  
The Cross

ABSTRACT Oritavancin is a lipoglycopeptide antibiotic that exhibits potent activities against vancomycin-resistant Gram-positive pathogens. Oritavancin differs from vancomycin by a hydrophobic side chain attached to the drug disaccharide, which forms a secondary binding site to enable oritavancin binding to the cross-linked peptidoglycan in the cell wall. The mode of action of secondary binding site was investigated by measuring the changes in the peptidoglycan composition of Staphylococcus aureus grown in the presence of desleucyl-oritavancin at subinhibitory concentration using liquid chromatography-mass spectrometry (LC-MS). Desleucyl-oritavancin is an Edman degradation product of oritavancin that exhibits potent antibacterial activities despite the damaged d-Ala–d-Ala binding site due to its functional secondary binding site. Accurate quantitative peptidoglycan composition analysis based on 83 muropeptide ions determined that cell walls of S. aureus grown in the presence of desleucyl-oritavancin showed a reduction of peptidoglycan cross-linking, increased muropeptides with a tetrapeptide-stem structure, decreased O-acetylation of MurNAc, and increased N-deacetylation of GlcNAc. The changes in peptidoglycan composition suggest that desleucyl-oritavancin targets the peptidoglycan template to induce cell wall disorder and interferes with cell wall maturation. IMPORTANCE Oritavancin is a lipoglycopeptide antibiotic with a secondary binding site that targets the cross-linked peptidoglycan bridge structure in the cell wall. Even after the loss of its primary d-Ala–d-Ala binding site through Edman degradation, desleucyl-oritavancin exhibits potent antimicrobial activities through its still-functioning secondary binding site. In this study, we characterized the mode of action for desleucyl-oritavancin's secondary binding site using LC-MS. Peptidoglycan composition analysis of desleucyl-oritavancin-treated S. aureus was performed by determining the relative abundances of 83 muropeptide ions matched from a precalculated library through integrating extracted ion chromatograms. Our work highlights the use of quantitative peptidoglycan composition analysis by LC-MS to provide insights into the mode of action of glycopeptide antibiotics.

Identification of phosphocysteine by electrospray mass spectrometry combined with Edman degradation

1995 ◽  
Vol 712 (1) ◽  
pp. 141-147 ◽  
Author(s):  
Christiane Weigt ◽  
Horst Korte ◽  
Rembert Pogge von Strandmann ◽  
Wolfgang Hengstenberg ◽  
Helmut E. Meyer
Keyword(s):  
Mass Spectrometry ◽  
Electrospray Mass Spectrometry ◽  
Edman Degradation
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