In this section
@article{Al:2026:10.1021/acsbiomedchemau.5c00237,
author = {Al, Musaimi O and Williams, DR},
doi = {10.1021/acsbiomedchemau.5c00237},
journal = {ACS Bio & Med Chem Au},
pages = {90--100},
title = {OBIMAP (One-Bead Interchain Multipeptide Assembly Platform)},
url = {http://dx.doi.org/10.1021/acsbiomedchemau.5c00237},
volume = {6},
year = {2026}
}
TY - JOUR
AB - 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 structuresranging from minimal cyclic dipeptides to small proteinsmany 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.
AU - Al,Musaimi O
AU - Williams,DR
DO - 10.1021/acsbiomedchemau.5c00237
EP - 100
PY - 2026///
SN - 2694-2437
SP - 90
TI - OBIMAP (One-Bead Interchain Multipeptide Assembly Platform)
T2 - ACS Bio & Med Chem Au
UR - http://dx.doi.org/10.1021/acsbiomedchemau.5c00237
UR - https://doi.org/10.1021/acsbiomedchemau.5c00237
VL - 6
ER -