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Chirality in Nature

Chirality in Nature

Chirality is the most intriguing yet essential facet of nature, governing life’s biochemical processes and precision. It can be observed from a snail shell pattern in a macroscopic world to an amino acid, the minutest building block of life. Most of the snails around the world have right-coiled shells because of the intrinsic chirality in their genes. All the amino acids present in the human body exist in an enantiomerically pure state, except for glycine - the sole achiral amino acid.

Prochirality

Prochirality

The concept of prochirality leads to the nomenclature of the individual faces of a molecule and plays a crucial role in the enantioselective reaction. It is a concept where two or more achiral molecules react to produce chiral products. A typical process is the reaction of an achiral ketone to generate a chiral alcohol. Here, the achiral reactant reacts with an achiral reducing agent, sodium borohydride, to generate an equimolar mixture of the chiral enantiomers of the product. For example, an...

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

Protein Folding

Protein Folding

Chirality at Nitrogen, Phosphorus, and Sulfur

Chirality at Nitrogen, Phosphorus, and Sulfur

Chirality is most prevalent in carbon-based tetrahedral compounds, but this important facet of molecular symmetry extends to sp3-hybridized nitrogen, phosphorus and sulfur centers, including trivalent molecules with lone pairs. Here, the lone pair behaves as a functional group in addition to the other three substituents to form an analogous tetrahedral center that can be chiral.
A consequence of chirality is the need for enantiomeric resolution. While this is theoretically possible for all...

Molecules with Multiple Chiral Centers

Molecules with Multiple Chiral Centers

Molecules that possess multiple chiral centers can afford a large number of stereoisomers. For instance, while some molecules like 2-butanol have one chiral center, defined as a tetrahedral carbon atom with four different substituents attached, several molecules like butane-2,3-diol have multiple chiral centers. A simple formula to predict the number of stereoisomers possible for a molecule with n chiral centers is 2n. However, there can be a lower number where some of the stereoisomers are...

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Related Experiment Video

Updated: Jan 10, 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

Controlling Supramolecular Assembly through Peptide Chirality.

Manosree Chatterjee^1,2,3, Itzhak Grinberg^1,2,3,4, Santu Bera^1,2,3

¹Department of Oral Biology, The Goldschleger School of Dental Medicine, The Gray Faculty of Medical and Health Sciences, Tel Aviv University, Tel Aviv 6997801, Israel.

ACS Applied Materials & Interfaces

|November 25, 2025

Summary

This summary is machine-generated.

Chirality significantly impacts peptide hydrogel formation. Enantiomeric design offers control over self-assembly kinetics and structure for enhanced biomolecule encapsulation and protection.

Keywords:

enantiomer hydrogel nanostructures peptide phase transition self-assembly

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

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Published on: November 21, 2013

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

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Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Published on: August 2, 2012

Area of Science:

Biomaterials Science
Supramolecular Chemistry
Materials Engineering

Background:

Peptide-based hydrogels, like fluorenylmethyloxycarbonyl-diphenylalanine (Fmoc-FF), offer biocompatibility and tunable properties.
Fmoc-FF hydrogels are promising for drug delivery and protecting oxygen-sensitive biomolecules.
Fast gelation of Fmoc-FF leads to structural heterogeneity, limiting applications.

Purpose of the Study:

To investigate the influence of chirality on Fmoc-FF hydrogel self-assembly kinetics and morphology.
To explore how enantiomeric composition affects hydrogel structural properties and functionality.
To assess the potential of enantiomerically designed hydrogels for encapsulating biomolecules and protecting oxygen-sensitive processes.

Main Methods:

Synthesis and characterization of all four enantiomeric forms of Fmoc-FF.
Utilized various analytical techniques to monitor self-assembly from monomers to nanostructures.
Encapsulated the oxygen-sensitive enzyme hydrogenase to assess hydrogel barrier properties.

Main Results:

Homoenantiomeric Fmoc-FF hydrogels showed faster gelation and increased rigidity.
Heteroenantiomeric systems exhibited a slower, three-phase gelation process with improved homogeneity.
All enantiomeric hydrogels effectively blocked oxygen diffusion, enabling hydrogenase activity.

Conclusions:

Chirality is a critical factor in controlling peptide hydrogel self-assembly and properties.
Slower gelation in heteroenantiomeric systems facilitates homogeneous cargo encapsulation.
Enantiomeric design provides a versatile strategy for developing advanced peptide hydrogels for diverse applications, including oxygen-sensitive processes.