Epitope Mapping with the Use of Peptide Libraries

Rodda, Stuart J.; Tribbick, Gordon; Geysen, Mario

doi:10.1002/9783527614912.ch10

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Cited by 2 publications

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“…Pin Synthesis [2,60,76,315] The polyethylene rods (diameter, 4 mm; length, 40 mm) immersed in a 6% (v/v) aqueous solution of acrylic acid were irradiated at a dose of 1 000 000 rads (1 rad ¼ 0.01 Gy). The rods so prepared were assembled into a polyethylene holder with the format and spacing of a microtiter plate.…”

Section: 61mentioning

confidence: 99%

Combinatorial/Library Peptide Synthesis

Lebl

2011

Amino Acids, Peptides and Proteins in Organic Chemistry

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Section: 61mentioning

confidence: 99%

Combinatorial/Library Peptide Synthesis

Lebl

2011

Amino Acids, Peptides and Proteins in Organic Chemistry

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Light‐Directed Simultaneous Synthesis of Oligopeptides on Microarray Substrate Using a Photogenerated Acid

Komolpis

Srivannavit

Gülari

2002

Biotechnology Progress

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Photogenerated acid (PGA) was used as the acid to remove the protection group from amino acids or peptide oligomers. Comparative study of the deprotection using a PGA, trisarylsulfonium antimonyhexafluoride (SSb), and trifluoroacetic acid (TFA) was performed on glass microscope slides. The results showed that PGA can replace TFA in the deprotection step of oligopeptide synthesis with comparable efficiencies. Acids needed for the deprotection step were generated in situ by light activation of the precursor molecule on the microwell substrate. A mask-less laser light illumination system was used to activate the precursor. The accuracy of the amino acid sequence of the synthesized oligopeptide and the location of the synthesis was illustrated by the specific recognition binding of two different models: lead(II) ion-peptide biosensor for lead(II) and human protein p53 (residue 20-25)-mouse MAb DO1. After parallel synthesis of the target peptide models and their analogues based on the predetermined pattern, specific binding treatment, and fluorescence labeling, the fluorescence emission images of the oligopeptide microarray showed fluorescence intensity as a result of specific binding at the correct locations of the array. The stepwise synthesis efficiencies of pentapeptide synthesis on the microwell substrate range are approximately 96-100% and do not decrease with respect to the chain length of the peptide.

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Epitope Mapping with the Use of Peptide Libraries

Cited by 2 publications

References 84 publications

Combinatorial/Library Peptide Synthesis

Combinatorial/Library Peptide Synthesis

Light‐Directed Simultaneous Synthesis of Oligopeptides on Microarray Substrate Using a Photogenerated Acid

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