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Related Concept Videos

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

Protein Organization

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

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...

Molecular Chaperones and Protein Folding

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

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Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

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Published on: January 26, 2016

Getting in shape: controlling peptide bioactivity and bioavailability using conformational constraints.

Jonathan E Bock¹, Jason Gavenonis¹, Joshua A Kritzer¹

¹Department of Chemistry, Tufts University, Medford, Massachusetts 02155, United States.

ACS Chemical Biology

|November 23, 2012

Summary

This summary is machine-generated.

Peptide conformation, not just physicochemical properties, is key to bioactivity and bioavailability. Understanding this peptide conformation-bioactivity link brings us closer to mimicking natural peptides.

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Area of Science:

Chemical Biology
Peptide Science
Drug Discovery

Background:

Traditionally, chemical biology focused on physicochemical properties to predict molecular behavior in biological systems.
A shift is occurring, recognizing conformation as a critical factor in peptide function.

Purpose of the Study:

To review emerging research linking peptide conformation to biological effects.
To explore how conformation influences cell penetration and intestinal absorption.
To assess the potential for mimicking natural peptide potency and bioavailability.

Main Methods:

Review of current scientific literature on peptide conformation and bioactivity.
Analysis of studies demonstrating the impact of conformational changes on peptide behavior.
Synthesis of findings related to cell penetration and absorption mechanisms.

Main Results:

Peptide conformation is emerging as the primary determinant of bioactivity and bioavailability.
Specific conformational states directly control biological effects, cell penetration, and intestinal absorption.
Evidence supports the feasibility of designing peptides with enhanced potency and bioavailability.

Conclusions:

Peptide conformation is a critical, actionable parameter for controlling biological activity.
Harnessing conformational control offers a pathway to developing peptide therapeutics with improved bioavailability.
The goal of achieving natural product-like peptide potency and bioavailability is increasingly attainable.