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Studies in solid-phase peptide synthesis: A personal perspective
✍ Scribed by Alexander R. Mitchell
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2007
- Tongue
- English
- Weight
- 272 KB
- Volume
- 90
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
By the early 1970s it had became apparent that the solid‐phase synthesis of ribonuclease A could not be generalized. Consequently, virtually every aspect of solid‐phase peptide synthesis (SPPS) was reexamined and improved during the decade of the 1970s. The sensitive detection and elimination of possible side reactions (amino acid insertion, N^α^‐trifluoroacetylation, N^αϵ^‐alkylation) were examined. The quantitation of coupling efficiency in SPPS as a function of chain length was studied. A new and improved support for SPPS, the “PAM‐resin,” was prepared and evaluated. These and many other studies from the Merrifield laboratory and elsewhere increased the general acceptance of SPPS leading to the 1984 Nobel Prize in Chemistry for Bruce Merrifield. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 90:215–233, 2008.
This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprintversion. You can request a copy of the preprint by emailing the Biopolymers editorial office at [email protected]
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## Abstract Bruce Merrifield, trained as a biochemist, had to address three major challenges related to the development and acceptance of solid‐phase peptide synthesis (SPPS). The challenges were (1) to reduce the concept of peptide synthesis on a insoluble support to practice, (2) overcome the res