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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...

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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.
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Signal Sequences and Sorting Receptors

Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...

Conservative Site-specific Recombination and Phase Variation

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Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
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Related Experiment Video

Updated: Mar 28, 2026

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids

Published on: September 21, 2017

Reversing the peptide sequence impacts on molecular surface behaviour.

Ernesto E Ambroggio¹, Benjamín Caruso¹, Marcos A Villarreal²

¹CIQUIBIC, CONICET, Departamento de Química Biológica, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Argentina.

Colloids and Surfaces. B, Biointerfaces

|December 25, 2015

Summary

Peptide sequence reversal significantly impacts amphiphilic peptide behavior at interfaces and their interaction with lipid bilayers. This sequence inversion alters surface properties and partitioning, demonstrating its critical role in molecular interactions.

Keywords:

Peptide Langmuir monolayer stability Peptide Langmuir rheology monolayer Peptide adsorption/penetration into interfaces Peptide retro-isomers Peptide/membrane interaction

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Area of Science:

Biochemistry
Materials Science
Surface Chemistry

Background:

Protein primary structure dictates folding and amphiphilic regions crucial for membrane interactions.
Understanding peptide sequence importance for surface properties is key to designing functional peptides.

Purpose of the Study:

To investigate how reversing peptide sequence (retro-isomerization) affects amphiphilic peptide surface properties and lipid interactions.
To determine the role of sequence order versus overall composition in peptide behavior.

Main Methods:

Design of three peptide pairs differing in hydrophilic residues and sequence.
Utilizing the Langmuir monolayer approach to analyze peptide monolayers at the air-water interface.
Employing Attenuated Total Reflectance Fourier-Transform Infrared Spectroscopy (ATR-FTIR) for secondary structure analysis.
Investigating peptide/lipid interactions with 1-palmitoyl-2-oleoyl-glycero-3-phosphocholine (POPC) lipid bilayers.

Main Results:

Sequence reversal critically influenced lateral stability, air-water interface partitioning, and rheological properties of peptide monolayers.
Secondary structure remained consistent across all designed peptides, irrespective of sequence.
Sequence inversion led to differential interactions between peptides and POPC lipid bilayers.

Conclusions:

Peptide sequence inversion significantly alters surface behavior and lipid interactions, even for molecules with similar hydrophobicity and secondary structure.
The primary sequence, not just composition, is a key determinant of amphiphilic peptide functionality at interfaces.