Large-Scale Analysis of Protein–Protein Interactions Using Cellulose-Bound Peptide Arrays

Beutling, Ulrike; Städing, Kai; Stradal, Theresia E. B.; Frank, Ronald

doi:10.1007/10_2008_096

Cited by 31 publications

(46 citation statements)

References 43 publications

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“…To define potential O4 binding regions in A42, peptide arrays 32 were produced and probed with the chemical compound ( Supplementary Fig. 5a, Fig.…”

Section: O4 Binds To Hydrophobic Regions In A42 Peptidesmentioning

confidence: 99%

Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrils

et al. 2011

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“…To define potential O4 binding regions in A42, peptide arrays 32 were produced and probed with the chemical compound ( Supplementary Fig. 5a, Fig.…”

Section: O4 Binds To Hydrophobic Regions In A42 Peptidesmentioning

confidence: 99%

Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrils

et al. 2011

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“…One solution could be to use peptide microarrays that could be prepared for a multitude of replicas. Pre-synthesized soluble peptides have been immobilized on glass slides using several methods [78][79][80][81]. However, the peptide microarray technique requires expensive equipment and special laboratory conditions.…”

Section: Resultsmentioning

confidence: 99%

Synthetic peptide arrays for investigating protein interaction domains

2012

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Synthetic peptide array technology was first developed in the early 1990s by Ronald Frank. Since then the technique has become a powerful tool for high throughput approaches in biology and biochemistry. Here, we focus on peptide arrays applied to investigate the binding specificity of protein interaction domains such as WW, SH3, and PDZ domains. We describe array‐based methods used to reveal domain networks in yeast, and briefly review rules as well as ideas about the synthesis and application of peptide arrays. We also provide initial results of a study designed to investigate the nature and evolution of SH3 domain interaction networks in eukaryotes.

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“…Peptide arrays were synthesized by the spot technique (38) on an amino-pegylated cellulose membrane (AIMS Scientific Products GmbH, Berlin, Germany) as described previously (45). Peptides are N-terminally acetylated and remain covalently attached to the membrane spot via their carboxyl terminus.…”

Section: Methodsmentioning

confidence: 99%

Application of Synthetic Peptide Arrays To Uncover Cyclic Di-GMP Binding Motifs

et al. 2016

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High levels of the universal bacterial second messenger cyclic di-GMP (c-di-GMP) promote the establishment of surface-attached growth in many bacteria. Not only can c-di-GMP bind to nucleic acids and directly control gene expression, but it also binds to a diverse array of proteins of specialized functions and orchestrates their activity. Since its development in the early 1990s, the synthetic peptide array technique has become a powerful tool for high-throughput approaches and was successfully applied to investigate the binding specificity of protein-ligand interactions. In this study, we used peptide arrays to uncover the c-di-GMP binding site of a Pseudomonas aeruginosa protein (PA3740) that was isolated in a chemical proteomics approach. PA3740 was shown to bind c-di-GMP with a high affinity, and peptide arrays uncovered LKKALKKQTNLR to be a putative c-di-GMP binding motif. Most interestingly, different from the previously identified c-di-GMP binding motif of the PilZ domain (RXXXR) or the I site of diguanylate cyclases (RXXD), two leucine residues and a glutamine residue and not the charged amino acids provided the key residues of the binding sequence. Those three amino acids are highly conserved across PA3740 homologs, and their singular exchange to alanine reduced c-di-GMP binding within the full-length protein.

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Large-Scale Analysis of Protein–Protein Interactions Using Cellulose-Bound Peptide Arrays

Abstract: Peptide arrays for screening large numbers of peptide fragments and probing with large numbers of samples is discussed.

Cited by 31 publications

References 43 publications

Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrils

Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrils

Synthetic peptide arrays for investigating protein interaction domains

Application of Synthetic Peptide Arrays To Uncover Cyclic Di-GMP Binding Motifs

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