ArticleJournal of the American Society for Mass Spectrometry2004
Detection of specific noncovalent interaction of peptide with DNA by MALDI-TOF.
Article in Journal of the American Society for Mass Spectrometry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 25 citations in OpenAlex.
- Insight into the binding of a non-toxic, self-assembling aromatic tripeptide with ct-DNA: Spectroscopic and viscositic studies.Biochemistry and biophysics reports · 2017Article
- Noncovalent complexes between DNA and basic polypeptides or polyamines by MALDI-TOF.Journal of the American Society for Mass Spectrometry · 2007Article
- A study of noncovalent complexes involving single-stranded DNA and polybasic compounds using nanospray mass spectrometry.Journal of the American Society for Mass Spectrometry · 2007Article
- Exploring the "intensity fading" phenomenon in the study of noncovalent interactions by MALDI-TOF mass spectrometry.Journal of the American Society for Mass Spectrometry · 2007Article
- Localization of noncovalent complexes in MALDI-preparations by CLSM.Journal of the American Society for Mass Spectrometry · 2006Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry was used to obtain spectra of peptide-DNA complexes formed by basic domain (BD15) of c-Fos protein and DNA AP-1 site (5'-TGAGTCA-3'). The noncovalent interaction between single stranded DNA and BD15 was observed and confirmed to be an ionic one between the negatively charged sugar-phosphate backbone of DNA and positively charged side chains of Arg- and lys-rich peptides as demonstrated by Vertes and coworkers and Woods and coworkers. But the specific noncovalent interaction between DNA AP-1 site and the dimer of BD15 was firstly detected in this paper. Various different sequence DNAs were studied and it was found that this interaction is a sequence-specific one, and AP-1 site was essential for this interaction. This specific interaction depends on the matrix. It was only observed in the ATT matrix and not in the other two matrixes (CHCA and DHBA).
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