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Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Related Experiment Video

Updated: Jun 29, 2026

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Published on: November 2, 2011

Peptide-Functionalized Rosette Nanotubes: Programmable Supramolecular Assembly and Tunable Peptide Surface

Alaaeddin Alsbaiee^1,2,3, Takeshi Yamazaki³, Mounir El Bakkari^2,3

¹Performance Materials Division, BASF Corporation, 1609 Biddle Avenue, Wyandotte, Michigan 48192, United States.

Biomacromolecules

|February 23, 2026

Summary

Researchers developed peptide-functionalized rosette nanotubes (RNTs) for programmable nanoscale organization. These RNTs offer a versatile platform for creating advanced biointerfaces by controlling peptide display on nanotubular surfaces.

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Last Updated: Jun 29, 2026

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

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Published on: November 2, 2011

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Published on: November 21, 2013

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Area of Science:

Supramolecular Chemistry
Nanotechnology
Materials Science

Background:

Rosette nanotubes (RNTs) are self-assembled nanostructures.
Previous studies explored RNTs, but peptide functionalization requires further investigation.

Purpose of the Study:

To investigate peptide-functionalized RNTs as scaffolds for programmable surface organization.
To understand how peptide identity affects nanotube assembly and surface structure.

Main Methods:

Conjugation of three distinct peptides to guanine-cytosine-inspired (G∧C) motifs.
Characterization using electron microscopy, spectroscopy, and molecular modeling.
Demonstration of coassembly with lysine-functionalized motifs.

Main Results:

Peptide-functionalized RNTs self-assembled robustly in aqueous media.
Peptide identity was shown to influence nanotube assembly and surface secondary structure.
Controllable coassembly allowed tunable peptide density and spatial distribution.

Conclusions:

Peptide identity dictates RNT assembly and surface properties.
RNTs serve as a versatile platform for designing nanoscale biointerfaces.
This study provides design principles for supramolecular peptide display on nanostructures.