Browse by author
Lookup NU author(s): Dr Othman AlmusaimiORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
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.
Author(s): Al Musaimi O, Williams DR
Publication type: Article
Publication status: Published
Journal: ACS Bio & Med Chem Au
Year: 2026
Pages: Epub ahead of print
Online publication date: 14/01/2026
Acceptance date: 07/01/2026
Date deposited: 03/02/2026
ISSN (electronic): 2694-2437
Publisher: American Chemical Society
URL: https://doi.org/10.1021/acsbiomedchemau.5c00237
DOI: 10.1021/acsbiomedchemau.5c00237
Data Access Statement: The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acsbiomedchemau.5c00237
Altmetrics provided by Altmetric
