Mass spectrometric analysis of a transition‐metal‐binding peptide using matrix‐assisted leaser‐desorption time‐of‐flight mass spectrometry. A demonstration of probe tip chemistry

Randall W. Nelson, T. William Hutchens

Research output: Contribution to journalArticle

54 Citations (Scopus)

Abstract

Matrix‐assisted laser desorption time‐of flight mass spectrometry has been used to investigate the affinity of aqueous copper ions for a 26‐residue synthetic peptide predicted to have metal‐binding properties. A specific reaction occurred upon the dirct application of aqueous CuSO4 to the matrix/peptide sample remaining on the probe tip ater initial mass spectrometric investigation. Results indicated the binding of up to one copper ion per histidine residue and the loss of one proton for each bound copper. Bound copper was not returned to solution upon subsequent cold water washings of the probe tip. These results suggest that covalent interations, between the copper and the peptide, occurred during the probe‐tip application of the metal ion to the sample.

Original languageEnglish (US)
Pages (from-to)4-8
Number of pages5
JournalRapid Communications in Mass Spectrometry
Volume6
Issue number1
DOIs
StatePublished - 1992

Fingerprint

Mass spectrometry
Copper
Demonstrations
Peptides
Ions
Histidine
Washing
Metal ions
Protons
Desorption
Water
Lasers

ASJC Scopus subject areas

  • Analytical Chemistry
  • Spectroscopy
  • Organic Chemistry

Cite this

@article{a58010a225044f648b119c8ca2fe9316,
title = "Mass spectrometric analysis of a transition‐metal‐binding peptide using matrix‐assisted leaser‐desorption time‐of‐flight mass spectrometry. A demonstration of probe tip chemistry",
abstract = "Matrix‐assisted laser desorption time‐of flight mass spectrometry has been used to investigate the affinity of aqueous copper ions for a 26‐residue synthetic peptide predicted to have metal‐binding properties. A specific reaction occurred upon the dirct application of aqueous CuSO4 to the matrix/peptide sample remaining on the probe tip ater initial mass spectrometric investigation. Results indicated the binding of up to one copper ion per histidine residue and the loss of one proton for each bound copper. Bound copper was not returned to solution upon subsequent cold water washings of the probe tip. These results suggest that covalent interations, between the copper and the peptide, occurred during the probe‐tip application of the metal ion to the sample.",
author = "Nelson, {Randall W.} and Hutchens, {T. William}",
year = "1992",
doi = "10.1002/rcm.1290060103",
language = "English (US)",
volume = "6",
pages = "4--8",
journal = "Rapid Communications in Mass Spectrometry",
issn = "0951-4198",
publisher = "John Wiley and Sons Ltd",
number = "1",

}

TY - JOUR

T1 - Mass spectrometric analysis of a transition‐metal‐binding peptide using matrix‐assisted leaser‐desorption time‐of‐flight mass spectrometry. A demonstration of probe tip chemistry

AU - Nelson, Randall W.

AU - Hutchens, T. William

PY - 1992

Y1 - 1992

N2 - Matrix‐assisted laser desorption time‐of flight mass spectrometry has been used to investigate the affinity of aqueous copper ions for a 26‐residue synthetic peptide predicted to have metal‐binding properties. A specific reaction occurred upon the dirct application of aqueous CuSO4 to the matrix/peptide sample remaining on the probe tip ater initial mass spectrometric investigation. Results indicated the binding of up to one copper ion per histidine residue and the loss of one proton for each bound copper. Bound copper was not returned to solution upon subsequent cold water washings of the probe tip. These results suggest that covalent interations, between the copper and the peptide, occurred during the probe‐tip application of the metal ion to the sample.

AB - Matrix‐assisted laser desorption time‐of flight mass spectrometry has been used to investigate the affinity of aqueous copper ions for a 26‐residue synthetic peptide predicted to have metal‐binding properties. A specific reaction occurred upon the dirct application of aqueous CuSO4 to the matrix/peptide sample remaining on the probe tip ater initial mass spectrometric investigation. Results indicated the binding of up to one copper ion per histidine residue and the loss of one proton for each bound copper. Bound copper was not returned to solution upon subsequent cold water washings of the probe tip. These results suggest that covalent interations, between the copper and the peptide, occurred during the probe‐tip application of the metal ion to the sample.

UR - http://www.scopus.com/inward/record.url?scp=84990677994&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84990677994&partnerID=8YFLogxK

U2 - 10.1002/rcm.1290060103

DO - 10.1002/rcm.1290060103

M3 - Article

VL - 6

SP - 4

EP - 8

JO - Rapid Communications in Mass Spectrometry

JF - Rapid Communications in Mass Spectrometry

SN - 0951-4198

IS - 1

ER -