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Related Concept Videos

Fibrous Proteins00:55

Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate filaments...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

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Related Experiment Video

Updated: May 13, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

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

Published on: November 21, 2013

Self-assembling multidomain peptide fibers with aromatic cores.

Erica L Bakota1, Ozge Sensoy, Beytullah Ozgur

  • 1Department of Chemistry, Rice University, 6100 South Main Street, Houston, Texas 77005, United States.

Biomacromolecules
|March 14, 2013
PubMed
Summary

Researchers modified self-assembling peptides by swapping amino acids. This altered hydrogen bonding and hydrogel properties, paving the way for advanced cell scaffolding materials.

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Area of Science:

  • Biomaterials science
  • Supramolecular chemistry
  • Materials engineering

Background:

  • Self-assembling multidomain peptides form shear-recoverable hydrogels.
  • Peptide properties like elasticity can be tuned via amino acid selection.
  • These peptides show potential for protein and cell encapsulation and delivery.

Purpose of the Study:

  • To investigate the impact of substituting aliphatic amino acids with aromatic amino acids (phenylalanine, tyrosine, tryptophan) in the central domain of self-assembling peptides.
  • To understand how these substitutions affect peptide self-assembly, nanofiber morphology, hydrogen bonding, and hydrogel rheological properties.

Main Methods:

  • Circular dichroism polarimetry
  • Infrared spectroscopy
  • Atomic force microscopy (AFM)
  • Transmission electron microscopy (TEM)
  • Scanning electron microscopy (SEM)
  • Oscillatory rheology
  • Molecular dynamics (MD) simulations

Main Results:

  • Basic nanofibrous morphology was maintained across all substitutions.
  • Substitution induced a switch from antiparallel to parallel hydrogen bonding.
  • Changes in nanofiber morphology and hydrogel rheological properties were observed based on core residue selection.

Conclusions:

  • Amino acid substitution in the central domain significantly alters peptide self-assembly and hydrogel characteristics.
  • The findings provide insights into designing next-generation peptide-based cell scaffolding materials with tunable properties.