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Updated: Jan 29, 2026

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

Proton-Transfer-Induced Fluorescence in Self-Assembled Short Peptides.

Sijo K Joseph^1,2, Natalia Kuritz¹, Eldad Yahel¹

¹Department of Physical Electronics , Tel-Aviv University , Tel-Aviv 69978 , Israel.

The Journal of Physical Chemistry. A

|February 13, 2019

Summary

This summary is machine-generated.

Photon-induced proton transfer in cyclic Phe-Phe dimers and trimers explains visible fluorescence in peptide nanostructures. This process is sensitive to hydrogen bond geometry.

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Area of Science:

* Biophysical Chemistry
* Computational Chemistry
* Molecular Spectroscopy

Background:

* Cyclic dipeptides, such as cyclic Phe-Phe (FF), are fundamental units in peptide nanostructures.
* Visible fluorescence in peptide assemblies is often experimentally observed but lacks a clear molecular explanation.
* Hydrogen bonding plays a critical role in the self-assembly and properties of peptide nanostructures.

Purpose of the Study:

* To investigate the molecular mechanisms underlying the visible fluorescence of cyclic FF molecules.
* To explore the role of proton transfer in excited states of FF dimers and trimers.
* To correlate specific hydrogen-bonding configurations with observed fluorescence properties.

Main Methods:

* Employed molecular dynamics (MD) simulations to model FF dimer and trimer structures.
* Utilized time-dependent density functional theory (TDDFT) to analyze excited-state properties and proton transfer.
* Analyzed the influence of geometrical arrangements on excited-state proton transfer (ESPT).

Main Results:

* Identified intra- and inter-molecular proton transfer in excited S1 and S2 states of specific FF configurations.
* Demonstrated that excited-state proton transfer (ESPT) within hydrogen bonds causes a significant red-shift in fluorescence.
* Showed that ESPT is highly sensitive to the precise geometry of hydrogen-bonded FF dimers and trimers.

Conclusions:

* Excited-state proton transfer in specific hydrogen-bonded configurations of cyclic FF molecules explains observed visible fluorescence.
* The findings provide a molecular basis for the fluorescence of β-sheet peptide nanostructures.
* Understanding the geometry-dependent nature of ESPT is crucial for designing fluorescent peptide materials.