Related Experiment Video
Updated: Oct 6, 2025
07:26
Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
13.1K
Heterochirality-Mediated Cross-Strand Nested Hydrophobic Interaction Effects Manifested in Surface-Bound Peptide
Yongfang Zheng1, Wendi Luo2, Lanlan Yu3
1Engineering Research Center of Industrial Biocatalysis, Fujian Province Universities, Fujian Provincial Key Laboratory of Advanced Materials Oriented Chemical Engineering, Fujian Provincial Key Laboratory of Polymer Materials, College of Chemistry and Materials Science, Fujian Normal University, Fuzhou 350007, P.R. China.
The Journal of Physical Chemistry. B
|January 14, 2022
Summary
Chirality in amino acids influences peptide self-assembly. Block heterochiral peptides, with alternating L- and D-amino acids, form more stable structures through enhanced side-chain packing in antiparallel beta-sheets.
Area of Science:
- Biochemistry
- Materials Science
- Supramolecular Chemistry
Background:
- Amino acid chirality is key for peptide self-assembly.
- Molecular mechanisms of chirality's role in peptide assemblies are not fully understood.
Purpose of the Study:
- To investigate the impact of block heterochirality on peptide assembly structures.
- To elucidate the molecular mechanisms behind chirality-induced structural stabilization.
Main Methods:
- Single-molecule characterization using scanning tunneling microscopy (STM).
- Analysis of self-assembly structures of L-polyphenylalanine (F10) and block heterochiral F5f5 peptides on highly oriented pyrolytic graphite (HOPG).
Main Results:
- Both F10 and F5f5 peptides formed distinct parallel and antiparallel beta-sheet structures.
- Antiparallel beta-sheets in F5f5 exhibited staggered side-chain packing, enhancing van der Waals interactions and stabilizing the assembly.
- This enhanced packing was not observed in parallel beta-sheets or enantiomerically pure assemblies.
Conclusions:
- Block heterochirality significantly enhances peptide assembly stability through specific side-chain interactions.
- Findings provide molecular insights into stereochemical effects in peptide assemblies.
- This strategy can be applied to design novel peptide architectures with tunable structures.
Related Concept Videos
01:25Protein Folding
9.5K
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 Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
9.5K
02:30Chirality in Nature
14.5K
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.
14.5K
02:04Protein-protein Interfaces
13.9K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
13.9K
01:13Protein Organization
148.9K
Overview
148.9K
02:35Noncovalent Attractions in Biomolecules
58.4K
Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
58.4K
02:05Prochirality
4.1K
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...
4.1K