Chemically derived peptide libraries: A new resin and methodology for lead identification

Buettner, Joseph A.; Dadd, Christopher A.; Baumbach, George A.; Masecar, Barbara L.; Hammond, David J.

doi:10.1111/j.1399-3011.1996.tb00812.x

Cited by 62 publications

(13 citation statements)

References 19 publications

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“…Peptide libraries were synthesized directly on Toyopearl AF‐Amino‐650 EC (particle size 100–300 μ m ) or M (particle size 65 μ m ) resins (Tosoh Bioscience Inc., Montgomeryville, PA, USA) with 18 of the 20 naturally occurring amino acids (except cysteine and methionine) using fluorenylmethyloxycarbonyl chemistry (19). In this paper, ‘large bead’ and ‘small bead’ libraries refer to the libraries built on EC and M resins, respectively.…”

Section: Methodsmentioning

confidence: 99%

Hexamer peptide affinity resins that bind the Fc region of human immunoglobulin G

Yang

Gurgel

Carbonell

2005

The Journal of Peptide Research

122

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A family of linear hexapeptides composed of histidine on the N‐terminus followed by aromatic amino acid(s) and positively charged amino acid(s) has been identified through a three‐step screening of a synthetic solid phase library. These peptides were able to recognize human immunoglobulin G (HIgG) through its Fc region, and their selectivity to Fc is comparable to Protein A. This is the first known report of short peptides that are able to bind HIgG by recognizing its Fc portion. One of the ligands from the identified family, HWRGWV, was examined for its ability to isolate HIgG from complex mixtures. It was found that HWRGWV possessed the potential to purify HIgG from complete mammalian cell culture medium containing 10% fetal calf serum with purity comparable to commercially available resins, but using milder elution conditions. HWRGWV bound all HIgG subclasses and IgGs from bovine, mouse, goat, and rabbit. The broad affinity spectrum as well as its Fc recognition ability may be useful in capturing and detecting both polyclonal and monoclonal antibodies.

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Section: Methodsmentioning

confidence: 99%

Hexamer peptide affinity resins that bind the Fc region of human immunoglobulin G

Yang

Gurgel

Carbonell

2005

The Journal of Peptide Research

122

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“…The CPLL were synthesized on beads by the splitcouple-recombine method described in earlier works (Furka et al, 1991;Lam et al, 1991;Buettner et al, 1996). Use of the 20 naturally occurring amino acids theoretically resulted in 64 million different ligands, with each ligand fixed to a single bead (Thulasiraman et al, 2005;Boschetti and Righetti, 2008a).…”

mentioning

confidence: 99%

Looking Deep Inside: Detection of Low-Abundance Proteins in Leaf Extracts of Arabidopsis and Phloem Exudates of Pumpkin

et al. 2012

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The field of proteomics suffers from the immense complexity of even small proteomes and the enormous dynamic range of protein concentrations within a given sample. Most protein samples contain a few major proteins, which hamper in-depth proteomic analysis. In the human field, combinatorial hexapeptide ligand libraries (CPLL; such as ProteoMiner) have been used for reduction of the dynamic range of protein concentrations; however, this technique is not established in plant research. In this work, we present the application of CPLL to Arabidopsis (Arabidopsis thaliana) leaf proteins. One-and two-dimensional gel electrophoresis showed a decrease in high-abundance proteins and an enrichment of less abundant proteins in CPLL-treated samples. After optimization of the CPLL protocol, mass spectrometric analyses of leaf extracts led to the identification of 1,192 proteins in control samples and an additional 512 proteins after the application of CPLL. Upon leaf infection with virulent Pseudomonas syringae DC3000, CPLL beads were also used for investigating the bacterial infectome. In total, 312 bacterial proteins could be identified in infected Arabidopsis leaves. Furthermore, phloem exudates of pumpkin (Cucurbita maxima) were analyzed. CPLL prefractionation caused depletion of the major phloem proteins 1 and 2 and improved phloem proteomics, because 67 of 320 identified proteins were detectable only after CPLL treatment. In sum, our results demonstrate that CPLL beads are a time-and cost-effective tool for reducing major proteins, which often interfere with downstream analyses. The concomitant enrichment of less abundant proteins may facilitate a deeper insight into the plant proteome.

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“…A year later, in 1996, another two-color approach was reported by Buettner et al (1996). The reported method allowed screening a library for the discovery of a peptide having affinity and specificity for human coagulation Factor IX.…”

Section: Evolution Of Dual Colormentioning

confidence: 95%

“…Another technique, as detailed below, consists in a double staining Buettner et al, 1996). Nonetheless, it is very difficult to eliminate all possible false-positive situations.…”

Section: Low-abundance Proteome Discoverymentioning

confidence: 98%

Other Applications of Combinatorial Peptide Libraries

Righetti¹,

Boschetti

2013

Low-Abundance Proteome Discovery

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Chemically derived peptide libraries: A new resin and methodology for lead identification

Cited by 62 publications

References 19 publications

Hexamer peptide affinity resins that bind the Fc region of human immunoglobulin G

Hexamer peptide affinity resins that bind the Fc region of human immunoglobulin G

Looking Deep Inside: Detection of Low-Abundance Proteins in Leaf Extracts of Arabidopsis and Phloem Exudates of Pumpkin

Other Applications of Combinatorial Peptide Libraries

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