Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...

You might also read

Related Articles

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

Sort by
Same author

N,N'-bridged heterocyclic bis-iminium salts as potent antimalarial agents against multi-resistant Plasmodium falciparum.

European journal of medicinal chemistry·2025
Same author

Delivering hydrosoluble compounds through the skin: what are the chances?

International journal of pharmaceutics·2023
Same author

Compounding and quality control of two pediatric topiramate pharmaceutical preparations.

Die Pharmazie·2021
Same author

Stockpiled N95 respirator/surgical mask release beyond manufacturer-designated shelf-life: a French experience.

The Journal of hospital infection·2020
Same author

Stability Studies of Antipyocyanic Beta-Lactam Antibiotics Used in Continuous Infusion.

Die Pharmazie·2019
Same author

Rituximab in relapsing and de novo MPO ANCA-associated vasculitis with severe renal involvement: a case series.

BMC nephrology·2019

Related Experiment Video

Updated: Jun 16, 2026

Preparing a 68Ga-labeled Arginine Glycine Aspartate (RGD)-peptide for Angiogenesis
07:48

Preparing a 68Ga-labeled Arginine Glycine Aspartate (RGD)-peptide for Angiogenesis

Published on: January 7, 2019

Targeting alphavbeta3 integrin: design and applications of mono- and multifunctional RGD-based peptides and

L Auzzas1, F Zanardi, L Battistini

  • 1Istituto di Chimica Biomolecolare del CNR, Traversa La Crucca 3, Li Punti, Sassari I-07100, Italy. luciana.auzzas@icb.cnr.it

Current Medicinal Chemistry
|February 20, 2010
PubMed
Summary

This review details the development of alpha(v)beta(3) integrin antagonists, focusing on cyclic RGD peptides. It covers their design, synthesis, and diverse biomedical applications in molecular medicine.

More Related Videos

Modification and Functionalization of the Guanidine Group by Tailor-made Precursors
09:45

Modification and Functionalization of the Guanidine Group by Tailor-made Precursors

Published on: April 27, 2017

Related Experiment Videos

Last Updated: Jun 16, 2026

Preparing a 68Ga-labeled Arginine Glycine Aspartate (RGD)-peptide for Angiogenesis
07:48

Preparing a 68Ga-labeled Arginine Glycine Aspartate (RGD)-peptide for Angiogenesis

Published on: January 7, 2019

Modification and Functionalization of the Guanidine Group by Tailor-made Precursors
09:45

Modification and Functionalization of the Guanidine Group by Tailor-made Precursors

Published on: April 27, 2017

Area of Science:

  • Biochemistry and Molecular Medicine
  • Drug Discovery and Development

Background:

  • Integrin receptors play a crucial physio-pathological role, driving significant global scientific interest.
  • Over twenty years of research have focused on the structural, functional, and biomedical applications of integrin antagonists.

Purpose of the Study:

  • To summarize efforts in designing, synthesizing, and applying cyclic RGD-containing alpha(v)beta(3) integrin antagonists.
  • To review both small and macromolecular formats of these antagonists.
  • To explore RGD-based multifunctional systems in molecular medicine.

Main Methods:

  • Review of literature on integrin inhibitor design and synthesis.
  • Analysis of biological and medical applications of monofunctional RGD ligands (monomeric and multimeric).
  • Evaluation of RGD-based multifunctional systems.

Main Results:

  • Elucidation of rational design principles for integrin inhibitors.
  • Demonstration of potent cyclic RGD-containing alpha(v)beta(3) integrin antagonists.
  • Exploration of diverse biomedical applications, including small and macromolecular formats.

Conclusions:

  • Cyclic RGD-containing alpha(v)beta(3) integrin antagonists represent a significant advancement in molecular medicine.
  • These antagonists show promise for various therapeutic applications.
  • Multifunctional RGD-based systems offer exciting potential for future research.