Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Clinical Supervision and Burnout Among Nurses: A Scoping Review.

Journal of advanced nursing·2026

Same author

RNApedia: a database of structural protein-RNA interactions.

Frontiers in bioinformatics·2026

Same author

Evaluation of metal-oxide semiconductors for the photocatalytic degradation of chloroquine phosphate in real-world water matrices.

Scientific reports·2026

Same author

Liposomes as delivery vectors for nucleic acid mimics into <i>Escherichia coli</i>: effect of composition and functionalization.

Frontiers in bioengineering and biotechnology·2026

Same author

Advances in Strategies to Transport Nanoparticles Across the Blood-Brain Barrier for Drug Delivery into the Brain for the Treatment of Alzheimer's Disease.

Pharmaceuticals (Basel, Switzerland)·2026

Same author

Solid lipid nanoparticles as carriers for <i>Ulva rigida</i> peptide extract with demonstrated anti-β-amyloid and antioxidant properties.

Frontiers in aging neuroscience·2026

Same journal

Multifunctional polysulfone/strontium silicate composites with tunable properties through silane functionalization.

Journal of materials chemistry. B·2026

Same journal

Melanocortin 1 receptor-targeted peptide-functionalized liposomes for enhanced melanocyte-preferential drug delivery and anti-melanogenic efficacy.

Journal of materials chemistry. B·2026

Same journal

Recent progress in side-chain amino acid-based polymers: synthesis, self-assembly, and emerging biomedical applications.

Journal of materials chemistry. B·2026

Same journal

Bioinspired electrospun nanofibrous dressings loaded with Mentha-derived exosome-like vesicles for antibacterial and immunomodulatory burn healing.

Journal of materials chemistry. B·2026

Same journal

On demand functionality of an NIR-enhanced nanozyme catalyst for infected wound healing.

Journal of materials chemistry. B·2026

Same journal

Positively charged, phenolic hydroxyl and anthraquinone structured polystyrene microspheres targeting dual elimination of bacterial pathogens and pathogen-associated molecular patterns for sepsis therapy.

Journal of materials chemistry. B·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Dec 24, 2025

A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation

A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation

Published on: January 9, 2019

Fluorinated beta-sheet breaker peptides.

Joana A Loureiro¹, Rosa Crespo, Hans Börner

¹LEPABE, Department of Chemical Engineering, Faculty of Engineering, University of Porto, Porto, Portugal. mcsp@fe.up.pt.

Journal of Materials Chemistry. B

|April 9, 2020

Summary

This summary is machine-generated.

Fluorinated amino acids effectively inhibit amyloid-β (Aβ) aggregation, a key factor in Alzheimer's disease. This research offers new peptide-based strategies to prevent amyloid fibril formation and combat the disease.

More Related Videos

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Published on: November 2, 2011

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide

Published on: December 19, 2020

Related Experiment Videos

Last Updated: Dec 24, 2025

A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation

A Fluorogenic Peptide Cleavage Assay to Screen for Proteolytic Activity: Applications for coronavirus spike protein activation

Published on: January 9, 2019

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets

Published on: November 2, 2011

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide

Published on: December 19, 2020

Area of Science:

Biochemistry
Neuroscience
Medicinal Chemistry

Background:

Amyloid-β (Aβ) peptide aggregation is a critical pathological hallmark of Alzheimer's disease, leading to neuritic plaque formation.
Developing inhibitors of Aβ aggregation is a primary therapeutic strategy for Alzheimer's disease.

Purpose of the Study:

To investigate the impact of incorporating fluorinated amino acids into peptide sequences on Aβ aggregation.
To explore novel peptide-based approaches for preventing amyloid fibril formation.

Main Methods:

Synthesis of peptides based on the LVFFD sequence with specific fluorinated amino acid substitutions.
Evaluation of the inhibitory effect of these modified peptides on Aβ aggregation.

Main Results:

Fluorination of hydrophobic residues, specifically valine or phenylalanine, significantly prevented Aβ aggregation.
Modified peptides demonstrated efficacy in inhibiting the formation of amyloid fibrils.

Conclusions:

Incorporating fluorinated amino acids into peptide sequences is a viable strategy to inhibit Aβ aggregation.
This study presents a promising avenue for developing new therapeutic agents targeting Alzheimer's disease through novel fluorinated peptide sequences.