Alewood, Paul, Alewood, Dianne, Miranda, Les, Love, Stephen, Meutermans, Wim, and Wilson, David (1997) Rapid in situ neutralization protocols for Boc and Fmoc solid-phase chemistries. Methods in Enzymology, 289. pp. 14-29.

PDF (Published Version) - Published Version Restricted to Repository staff only

Abstract

The protocols for Boc chemistry are characterized by the use of a single and inexpensive solvent dimethylformamide (DMF), to maintain maximum solvation of the peptide-resin. This ensures swelling of the peptide-resin while potentially aiding the disaggregation of intermolecularly H-bonded aggregates, a major contributor to "difficult sequences." Rapid flow washes of the swollen peptide-resin, combined with high concentrations (0.3–0.5 M) of activated amino acids and in situ neutralization, provide improved coupling efficiencies. Together with modern analytical techniques for peptide analysis such as mass spectrometry (MS) and MS combined with liquid chromatography (LC–MS), it is now feasible to observe and determine the nature of the various side products in solid-phase peptide synthesis (SPPS). Such analyses are critical for future improvements in peptide synthesis.

Item ID:	39316
Item Type:	Article (Research - C1)
ISBN:	978-0-12-182190-6
ISSN:	1557-7988
Keywords:	biochemical research methods; biochemistry & molecular biology; amino deprotecting procedure; peptide-synthesis; sequences; proteins
Funders:	Australian Research Council (ARC)
Date Deposited:	13 Mar 2017 00:43
FoR Codes:	03 CHEMICAL SCIENCES > 0304 Medicinal and Biomolecular Chemistry > 030406 Proteins and Peptides @ 100%
SEO Codes:	97 EXPANDING KNOWLEDGE > 970103 Expanding Knowledge in the Chemical Sciences @ 100%
Downloads:	Total: 1
	More Statistics