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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...

Peptide Identification Using Tandem Mass Spectrometry

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...

Fibrous Proteins

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...

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

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...

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Author Spotlight: Optimization of Ultrashort Peptide Matrices for Colorectal Cancer Organoids

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Biomaterials Made from Coiled-Coil Peptides.

Vincent Conticello¹, Spencer Hughes², Charles Modlin²

¹Emory University Chemistry Department, 1515 Dickey Drive, Atlanta, 30322, Georgia. vcontic@emory.edu.

Sub-Cellular Biochemistry

|January 20, 2017

Summary

Researchers are creating advanced biomaterials using coiled-coil proteins for personalized medicine. These protein-based biomaterials offer specific functions, bridging scientific discovery and technological applications.

Keywords:

Biomaterials Coiled-coils Hydrogels Nanomedicine Nanotubes

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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

Area of Science:

Biomaterials Science
Protein Engineering
Personalized Medicine

Background:

Biomaterials development is crucial for personalized medicine, but achieving highly specific functions remains a challenge.
Molecular structure dictates biomaterial function, with proteins offering unique design possibilities due to their specificity.
Coiled-coils are well-understood protein structural motifs with inherent diversity and tunability.

Purpose of the Study:

To survey biomaterials constructed from coiled-coil protein structures.
To discuss the utility of coiled-coils for creating novel, functional biomaterials.
To illustrate progress in coiled-coil biomaterials, linking academic research to technological impact.

Main Methods:

Review of scientific literature on coiled-coil protein structures.
Analysis of studies demonstrating the rational design of coiled-coil biomaterials.
Case studies showcasing the transition from scientific concept to potential application.

Main Results:

Coiled-coil proteins serve as versatile building blocks for functional biomaterials.
The structural diversity and tunable nature of coiled-coils enable specific functionalities.
Significant progress has been made in developing coiled-coil biomaterials with potential technological applications.

Conclusions:

Coiled-coil proteins are highly promising for the rational design of advanced biomaterials.
These biomaterials hold potential for significant impact in personalized medicine and beyond.
Further research can bridge the gap between coiled-coil biomaterial science and real-world applications.