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Aquaporins

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Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.

Peptide Bonds

Peptide Bonds

A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...

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Updated: Dec 30, 2025

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Accelerated charge transfer in water-layered peptide assemblies.

Kai Tao¹, Joseph O' Donnell², Hui Yuan³

¹Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 6997801, Israel.

Energy & Environmental Science

|January 25, 2020

Summary

Researchers developed novel bioinspired assemblies using water and peptide layers for enhanced energy storage. These structures exhibit piezoelectric properties, offering new avenues for improving charge transfer in biomolecular systems.

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Published on: February 27, 2019

Area of Science:

Supramolecular chemistry
Materials science
Bioinspired engineering

Background:

Bioinspired assemblies show promise for energy applications.
Biological molecules face limitations in efficient charge transfer.

Purpose of the Study:

To create novel bioinspired architectures for enhanced charge transfer.
To explore piezoelectric properties in water-peptide assemblies.

Main Methods:

Assembling l-tryptophan-d-tryptophan into alternating water and peptide layers.
Investigating dipole-dipole interactions and piezoelectric response.
Employing doping strategies like iodine adsorption and isotope replacement.

Main Results:

The assembled architectures exhibit significant piezoelectric response due to extensive water molecule connections.
Doping via iodine adsorption or isotope replacement effectively engineered charge transfer without altering chemical composition.
Demonstrated a simple system for enhancing charge transfer in bioinspired materials.

Conclusions:

Novel water-peptide layered assemblies offer a promising platform for energy generation and storage.
Engineered piezoelectricity and doping strategies provide new solutions for charge transfer enhancement.
This work advances the field of bioinspired supramolecular architectures for energy applications.