OBIMAP (One-Bead Interchain Multipeptide Assembly Platform)
File(s)
Published online version
Author(s)
Al Musaimi, Othman
Williams, Daryl R
Type
Journal Article
Abstract
A significant advancement in Merrifield’s classic solid-phase peptide synthesis (SPPS) that greatly expands the scope of accessible peptide structures is reported here. Building upon the one-bead, one-compound (OBOC) concept, this approach enables the simultaneous synthesis of multiple peptides on a single bead, followed by a novel solid-phase interchain assembly reaction to produce the final peptide product. This method, the one-bead interchain multipeptide assembly platform (OBIMAP), successfully generates diverse peptide architectures, including linear, cyclic, and bicyclic structures─ranging from minimal cyclic dipeptides to small proteins─many of which are inaccessible through conventional SPPS. OBIMAP demonstrates superior efficiency in both time and product purity compared to traditional methods. Crucially, it eliminates the need for solution-phase fragment condensation, a common but cumbersome step commonly used in synthesizing therapeutic peptides (30–60 amino acids). In addition to enhancing conventional SPPS methodologies, the OBIMAP enables access to novel classes of peptide architectures, including highly constrained peptides that were previously considered synthetically inaccessible.
Date Issued
2026-02-18
Date Acceptance
2026-01-07
Citation
ACS Bio & Med Chem Au, 2026, 6 (1), pp.90-100
ISSN
2694-2437
Publisher
American Chemical Society
Start Page
90
End Page
100
Journal / Book Title
ACS Bio & Med Chem Au
Volume
6
Issue
1
Copyright Statement
© 2026 The Authors. Published by American Chemical Society. This publication is licensed under CC-BY 4.0 .
License URL
Publication Status
Published
Date Publish Online
2026-01-14